M00199
type: Enzyme
rlcp: p10765
rlcp: p352
rlcp: p10590
cath: Rossmann fold
cath: Nitrogenase Molybdenum-iron Protein, subunit B; domain 4
ec: https://purl.uniprot.org/enzyme/1.18.6.1
uniprot: P00467
uniprot: P11347
uniprot: P00456
kegg enzyme: nitrogenase
kegg pathway: Tetrachloroethene degradation
kegg pathway: Nitrogen metabolism
kegg cofactor: [8Fe-7S](P cluster)
kegg cofactor: [7Fe-9S-Mo](FeMoco)
kegg cofactor: Homocitrate
kegg cofactor: [4Fe-4S]
kegg cofactor: Magnesium
kegg substrate: Reduced ferredoxin
kegg substrate: H+
kegg substrate: N2
kegg substrate: ATP
kegg substrate: H2O
kegg product: Oxidized ferredoxin
kegg product: NH3
kegg product: ADP
kegg product: Orthophosphate
pdb: 1mioA01
pdb: 1mioC01
pdb: 1mioA02
pdb: 1mioC02
pdb: 1mioA03
pdb: 1mioC03
pdb: 1mioB01
pdb: 1mioD01
pdb: 1mioB02
pdb: 1mioD02
pdb: 1mioB04
pdb: 1mioD04
pdb: 1mioB03
pdb: 1mioD03
pdb: 1cp2A
pdb: 1cp2B
references: Nitrogenase XII. Mossbauer studies of the MoFe protein from Clostridium pasteurianum W5.
references: Neutron small angle scattering of the Mo-Fe protein (nitrogenase) from Clostridium pasteurianum.
references: Molecular symmetry of the MoFe protein of nitrogenase. Structural homology/nitrogen fixation/x-ray crystallography.
references: Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii.
references: Molecular basis of biological nitrogen fixation.
references: Distinct structural features of the alpha and beta subunits of nitrogenase molybdenum-iron protein of Clostridium pasteurianum: an analysis of amino acid sequences.
references: Comparison of redox and EPR properties of the molybdenum iron proteins of Clostridium pasteurianum and Azotobacter vinelandii nitrogenases.
references: Hydrogen-1 nuclear magnetic resonance of the nitrogenase iron protein (Cp2) from Clostridium pasteurianum.
references: E.p.r.-spectroscopic studies on the molybdenum-iron site of nitrogenase from Clostridium pasteurianum.
references: Role for the nitrogenase MoFe protein alpha-subunit in FeMo-cofactor binding and catalysis.
references: Pulsed electron paramagnetic resonance studies of the interaction of Mg-ATP and D2O with the iron protein of nitrogenase.
references: Metalloclusters of the nitrogenases.
references: Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii.
references: Structural models for the metal centers in the nitrogenase molybdenum-iron protein.
references: Ionic interactions in the nitrogenase complex. Properties of Fe-protein containing substitutions for Arg-100.
references: Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii.
references: Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125.
references: The role of metal clusters and MgATP in nitrogenase catalysis.
references: Molybdenum-independent nitrogenases of Azotobacter vinelandii: a functional species of alternative nitrogenase-3 isolated from a molybdenum-tolerant strain contains an iron-molybdenum cofactor.
references: X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution.
references: Using dysprosium complexes to probe the nitrogenase paramagnetic centers.
references: The nitrogenase MoFe protein. A secondary structure prediction.
references: The unusual metal clusters of nitrogenase: structural features revealed by x-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum.
references: The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures.
references: Functional mimics of vanadium enzymes.
references: Purification and characterization of a FeMo cofactor-deficient MoFe protein.
references: MgATP-induced conformational changes in the iron protein from Azotobacter vinelandii, as studied by small-angle x-ray scattering.
references: Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein.
references: Catalytic formation of a nitrogenase iron-sulfur cluster.
references: Docking of nitrogenase iron- and molybdenum-iron proteins for electron transfer and MgATP hydrolysis: the role of arginine 140 and lysine 143 of the Azotobacter vinelandii iron protein.
references: Nitrogenase structure and function: a biochemical-genetic perspective.
references: Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis.
references: Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe protein.
references: Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
references: Nucleotide hydrolysis and protein conformational changes in Azotobacter vinelandii nitrogenase iron protein: defining the function of aspartate 129.
references: Evidence for a central role of lysine 15 of Azotobacter vinelandii nitrogenase iron protein in nucleotide binding and protein conformational changes.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1980
catalytic domain: index.html

Nitrogenase Molybdenum-iron Protein, subunit B; domain 4
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.89.10

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.300
catalytic domain: index.html

Tetrachloroethene degradation
type: KeggPathway
references: KEGG:MAP00625

Nitrogen metabolism
type: KeggPathway
references: KEGG:MAP00910

[8Fe-7S](P cluster)
type: KeggCofactor
references: KEGG:L00026
compound type: heavy metal
compound type: sulfide group

[7Fe-9S-Mo](FeMoco)
type: KeggCofactor
references: KEGG:L00025
references: CHEBI:48796
compound type: heavy metal
compound type: sulfide group

Homocitrate
type: KeggCofactor
references: KEGG:C01251
references: CHEBI:52222
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: carboxyl group

[4Fe-4S]
type: KeggCofactor
references: KEGG:L00024
references: CHEBI:33725
compound type: heavy metal
compound type: sulfide group

Magnesium
type: KeggCofactor
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: divalent metal (Ca2+, Mg2+)

Reduced ferredoxin
type: KeggSubstrate
references: KEGG:C00138
compound type: heavy metal
compound type: peptide/protein
compound type: sulfide group

H+
type: KeggSubstrate
references: KEGG:C00080
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: others

N2
type: KeggSubstrate
references: KEGG:C00697
references: CHEBI:17997
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: others

ATP
type: KeggSubstrate
references: KEGG:C00002
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: nucleotide

H2O
type: KeggSubstrate
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: H2O

Oxidized ferredoxin
type: KeggProduct
references: KEGG:C00139
compound type: heavy metal
compound type: peptide/protein
compound type: sulfide group

NH3
type: KeggProduct
references: KEGG:C00014
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: organic ion

ADP
type: KeggProduct
references: KEGG:C00008
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: nucleotide

Orthophosphate
type: KeggProduct
references: KEGG:C00009
references: CHEBI:26078
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: phosphate group/phosphate ion

1mioA01
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
catalytic residue: CYS 53
cofactor binding residue: CYS 53(P cluster);ILE 465;HIS 482(Homocitrate);HIS 482(FeMoco)

1mioC01
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
catalytic residue: CYS 53
cofactor binding residue: CYS 53(P cluster);ILE 465;HIS 482(Homocitrate);HIS 482(FeMoco)

1mioA02
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
catalytic residue: GLN 182
cofactor binding residue: GLN 182(Homocitrate);CYS 79;CYS 145(P cluster)

1mioC02
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
catalytic residue: GLN 182
cofactor binding residue: GLN 182(Homocitrate);CYS 79;CYS 145(P cluster)

1mioA03
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
cofactor binding residue: CYS 262(FeMoco)

1mioC03
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
cofactor binding residue: CYS 262(FeMoco)

1mioB01
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
catalytic residue: CYS 106;THR 110
cofactor binding residue: CYS 23;CYS 48;CYS 106;SER 141(P cluster)

1mioD01
type: Pdb
references: 1mio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mio
catalytic residue: CYS 106;THR 110
cofactor binding residue: CYS 23;CYS 48;CYS 106;SER 141(P cluster)

1cp2A
type: Pdb
references: 1cp2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cp2
catalytic residue: LYS 9;LYS 14;ASP 38;LYS 40;ASP 126
cofactor binding residue: CYS 94;CYS 129(4Fe-4S binding);SER 15(Magnesium binding)
main chain in catalysis: GLY 11

1cp2B
type: Pdb
references: 1cp2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cp2
catalytic residue: LYS 9;LYS 14;ASP 38;LYS 40;ASP 126
cofactor binding residue: CYS 94;CYS 129(4Fe-4S binding);SER 15(Magnesium binding)
main chain in catalysis: GLY 11

Nitrogenase XII. Mossbauer studies of the MoFe protein from Clostridium pasteurianum W5.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6246963
journal: Biochim Biophys Acta
volume: 623
pages: 124-38
published year: 1980
authors:
  item: Huynh BH
  item: Henzl MT
  item: Christner JA
  item: Zimmermann R
  item: Orme-Johnson WH
  item: Munck E

Neutron small angle scattering of the Mo-Fe protein (nitrogenase) from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6938202
journal: Biochem Biophys Res Commun
volume: 98
pages: 43-50
published year: 1981
authors:
  item: Meyer J
  item: Zaccai G

Molecular symmetry of the MoFe protein of nitrogenase. Structural homology/nitrogen fixation/x-ray crystallography.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6948813
journal: J Biol Chem
volume: 257
pages: 1221-3
published year: 1982
authors:
  item: Yamane T
  item: Weininger MS
  item: Mortenson LE
  item: Rossmann MG

Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6952190
journal: Proc Natl Acad Sci U S A
volume: 79
pages: 378-80
published year: 1982
authors:
  item: Weininger MS
  item: Mortenson LE

Molecular basis of biological nitrogen fixation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3890886
journal: Annu Rev Biophys Biophys Chem
volume: 14
pages: 419-59
published year: 1985
authors:
  item: Orme-Johnson WH

Distinct structural features of the alpha and beta subunits of nitrogenase molybdenum-iron protein of Clostridium pasteurianum: an analysis of amino acid sequences.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2840948
journal: Biochemistry
volume: 27
pages: 2800-10
published year: 1988
authors:
  item: Wang SZ
  item: Chen JS
  item: Johnson JL

Comparison of redox and EPR properties of the molybdenum iron proteins of Clostridium pasteurianum and Azotobacter vinelandii nitrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2842451
journal: J Inorg Biochem
volume: 33
pages: 111-20
published year: 1988
authors:
  item: Morgan TV
  item: Mortenson LE
  item: McDonald JW
  item: Watt GD

Hydrogen-1 nuclear magnetic resonance of the nitrogenase iron protein (Cp2) from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2847787
journal: Biochemistry
volume: 27
pages: 6150-6
published year: 1988
authors:
  item: Meyer J
  item: Gaillard J
  item: Moulis JM

E.p.r.-spectroscopic studies on the molybdenum-iron site of nitrogenase from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2554893
journal: Biochem J
volume: 262
pages: 349-52
published year: 1989
authors:
  item: George GN
  item: Bare RE
  item: Jin HY
  item: Stiefel EI
  item: Prince RC

Role for the nitrogenase MoFe protein alpha-subunit in FeMo-cofactor binding and catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2153269
journal: Nature
volume: 343
pages: 188-90
published year: 1990
authors:
  item: Scott DJ
  item: May HD
  item: Newton WE
  item: Brigle KE
  item: Dean DR

Pulsed electron paramagnetic resonance studies of the interaction of Mg-ATP and D2O with the iron protein of nitrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2159783
journal: Biochemistry
volume: 29
pages: 3077-82
published year: 1990
authors:
  item: Morgan TV
  item: McCracken J
  item: Orme-Johnson WH
  item: Mims WB
  item: Mortenson LE
  item: Peisach J

Metalloclusters of the nitrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1555570
journal: Eur J Biochem
volume: 205
pages: 1-15
published year: 1992
authors:
  item: Smith BE
  item: Eady RR

Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
journal: Nature
volume: 360
pages: 553-60
published year: 1992
authors:
  item: Kim J
  item: Rees DC
references: P07328
references: P07329

Structural models for the metal centers in the nitrogenase molybdenum-iron protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1529354
journal: Science
volume: 257
pages: 1677-82
published year: 1992
authors:
  item: Kim J
  item: Rees DC

Ionic interactions in the nitrogenase complex. Properties of Fe-protein containing substitutions for Arg-100.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1740419
journal: J Biol Chem
volume: 267
pages: 3667-73
published year: 1992
authors:
  item: Wolle D
  item: Kim C
  item: Dean D
  item: Howard JB

Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
medline id: 92410322
references: http://www.ncbi.nlm.nih.gov/pubmed/1529353
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00459
journal: Science
volume: 257
pages: 1653-9
published year: 1992
authors:
  item: Georgiadis MM
  item: Komiya H
  item: Chakrabarti P
  item: Woo D
  item: Kornuc JJ
  item: Rees DC

Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1359643
journal: Science
volume: 258
pages: 992-5
published year: 1992
authors:
  item: Wolle D
  item: Dean DR
  item: Howard JB

The role of metal clusters and MgATP in nitrogenase catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8322617
journal: Adv Enzymol Relat Areas Mol Biol
volume: 67
pages: 299-374
published year: 1993
authors:
  item: Mortenson LE
  item: Seefeldt LC
  item: Morgan TV
  item: Bolin JT

Molybdenum-independent nitrogenases of Azotobacter vinelandii: a functional species of alternative nitrogenase-3 isolated from a molybdenum-tolerant strain contains an iron-molybdenum cofactor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8392330
journal: Biochem J
volume: 293
pages: 101-7
published year: 1993
authors:
  item: Pau RN
  item: Eldridge ME
  item: Lowe DJ
  item: Mitchenall LA
  item: Eady RR

X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS
medline id: 93344379
references: http://www.ncbi.nlm.nih.gov/pubmed/8393705
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00467
references: P11347
journal: Biochemistry
volume: 32
pages: 7104-15
published year: 1993
authors:
  item: Kim J
  item: Woo D
  item: Rees DC

Using dysprosium complexes to probe the nitrogenase paramagnetic centers.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8389587
journal: Biochemistry
volume: 32
pages: 6058-64
published year: 1993
authors:
  item: Oliver ME
  item: Hales BJ

The nitrogenase MoFe protein. A secondary structure prediction.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8440368
journal: FEBS Lett
volume: 318
pages: 118-24
published year: 1993
authors:
  item: Gerloff DL
  item: Jenny TF
  item: Knecht LJ
  item: Gonnet GH
  item: Benner SA

The unusual metal clusters of nitrogenase: structural features revealed by x-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8430077
journal: Proc Natl Acad Sci U S A
volume: 90
pages: 1078-82
published year: 1993
authors:
  item: Bolin JT
  item: Ronco AE
  item: Morgan TV
  item: Mortenson LE
  item: Xuong NH

The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8484118
journal: Science
volume: 260
pages: 792-4
published year: 1993
authors:
  item: Chan MK
  item: Kim J
  item: Rees DC

Functional mimics of vanadium enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8140948
journal: Adv Inorg Biochem
volume: 9
pages: 219-43
published year: 1994
authors:
  item: Clague MJ
  item: Butler A

Purification and characterization of a FeMo cofactor-deficient MoFe protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7918402
journal: Biochemistry
volume: 33
pages: 11842-9
published year: 1994
authors:
  item: Gavini N
  item: Ma L
  item: Watt G
  item: Burgess BK

MgATP-induced conformational changes in the iron protein from Azotobacter vinelandii, as studied by small-angle x-ray scattering.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8106367
journal: J Biol Chem
volume: 269
pages: 3290-4
published year: 1994
authors:
  item: Chen L
  item: Gavini N
  item: Tsuruta H
  item: Eliezer D
  item: Burgess BK
  item: Doniach S
  item: Hodgson KO

Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7961744
journal: J Biol Chem
volume: 269
pages: 28076-83
published year: 1994
authors:
  item: Peters JW
  item: Fisher K
  item: Dean DR

Catalytic formation of a nitrogenase iron-sulfur cluster.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8034623
journal: J Biol Chem
volume: 269
pages: 18723-6
published year: 1994
authors:
  item: Zheng L
  item: Dean DR

Docking of nitrogenase iron- and molybdenum-iron proteins for electron transfer and MgATP hydrolysis: the role of arginine 140 and lysine 143 of the Azotobacter vinelandii iron protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7703853
journal: Protein Sci
volume: 3
pages: 2073-81
published year: 1994
authors:
  item: Seefeldt LC

Nitrogenase structure and function: a biochemical-genetic perspective.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8561464
journal: Annu Rev Microbiol
volume: 49
pages: 335-66
published year: 1995
authors:
  item: Peters JW
  item: Fisher K
  item: Dean DR

Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7893691
journal: Biochemistry
volume: 34
pages: 2798-808
published year: 1995
authors:
  item: Kim CH
  item: Newton WE
  item: Dean DR

Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7592949
journal: J Biol Chem
volume: 270
pages: 27007-13
published year: 1995
authors:
  item: Peters JW
  item: Fisher K
  item: Newton WE
  item: Dean DR

Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7495793
journal: Biochemistry
volume: 34
pages: 15646-53
published year: 1995
authors:
  item: Lanzilotta WN
  item: Holz RC
  item: Seefeldt LC

Nucleotide hydrolysis and protein conformational changes in Azotobacter vinelandii nitrogenase iron protein: defining the function of aspartate 129.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7662655
journal: Biochemistry
volume: 34
pages: 10713-23
published year: 1995
authors:
  item: Lanzilotta WN
  item: Ryle MJ
  item: Seefeldt LC

Evidence for a central role of lysine 15 of Azotobacter vinelandii nitrogenase iron protein in nucleotide binding and protein conformational changes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7768906
journal: J Biol Chem
volume: 270
pages: 13112-7
published year: 1995
authors:
  item: Ryle MJ
  item: Lanzilotta WN
  item: Mortenson LE
  item: Watt GD
  item: Seefeldt LC

Isolation of two forms of the nitrogenase VFe protein from Azotobacter vinelandii.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8555217
journal: Biochemistry
volume: 35
pages: 472-8
published year: 1996
authors:
  item: Blanchard CZ
  item: Hales BJ

Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: characterization of a tight protein-protein complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8679547
journal: Biochemistry
volume: 35
pages: 7188-96
published year: 1996
authors:
  item: Lanzilotta WN
  item: Fisher K
  item: Seefeldt LC

Electron transfer from the nitrogenase iron protein to the [8Fe-(7/8)S] clusters of the molybdenum-iron protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8988014
journal: Biochemistry
volume: 35
pages: 16770-6
published year: 1996
authors:
  item: Lanzilotta WN
  item: Seefeldt LC

Oxidative titration of the nitrogenase VFe protein from Azotobacter vinelandii: an example of redox-gated electron flow.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8555218
journal: Biochemistry
volume: 35
pages: 479-87
published year: 1996
authors:
  item: Tittsworth RC
  item: Hales BJ

Elucidating the mechanism of nucleotide-dependent changes in the redox potential of the [4Fe-4S] cluster in nitrogenase iron protein: the role of phenylalanine 135.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8755721
journal: Biochemistry
volume: 35
pages: 9424-34
published year: 1996
authors:
  item: Ryle MJ
  item: Lanzilotta WN
  item: Seefeldt LC

The [4Fe-4S] cluster domain of the nitrogenase iron protein facilitates conformational changes required for the cooperative binding of two nucleotides.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8961928
journal: Biochemistry
volume: 35
pages: 15654-62
published year: 1996
authors:
  item: Ryle MJ
  item: Seefeldt LC

Elucidation of a MgATP signal transduction pathway in the nitrogenase iron protein: formation of a conformation resembling the MgATP-bound state by protein engineering.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8664266
journal: Biochemistry
volume: 35
pages: 4766-75
published year: 1996
authors:
  item: Ryle MJ
  item: Seefeldt LC

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00199#44
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8576152
journal: J Biol Chem
volume: 271
pages: 1551-7
published year: 1996
authors:
  item: Ryle MJ
  item: Lanzilotta WN
  item: Seefeldt LC
  item: Scarrow RC
  item: Jensen GM
title: Circular dichroism and x-ray spectroscopies of Azotobacter vinelandii nitrogenase iron protein. MgATP and MgADP induced protein conformational changes affecting the [4Fe-4S] cluster and characterization of a [2Fe-2S] form.

Nitrogenase of Klebsiella pneumoniae: kinetics of formation of the transition-state complex and evidence for an altered conformation of MoFe protein lacking a FeMoco centre.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9307010
journal: Biochem J
volume: 326
pages: 637-40
published year: 1997
authors:
  item: Yousafzai FK
  item: Eady RR

Changes in the midpoint potentials of the nitrogenase metal centers as a result of iron protein-molybdenum-iron protein complex formation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9335558
journal: Biochemistry
volume: 36
pages: 12976-83
published year: 1997
authors:
  item: Lanzilotta WN
  item: Seefeldt LC

Redox-dependent structural changes in the nitrogenase P-cluster.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
medline id: 97178802
references: http://www.ncbi.nlm.nih.gov/pubmed/9063865
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07328
references: P07329
journal: Biochemistry
volume: 36
pages: 1181-7
published year: 1997
authors:
  item: Peters JW
  item: Stowell MH
  item: Soltis SM
  item: Finnegan MG
  item: Johnson MK
  item: Rees DC

Structural analysis of the Trichodesmium nitrogenase iron protein: implications for aerobic nitrogen fixation activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9271856
journal: FEMS Microbiol Lett
volume: 153
pages: 303-9
published year: 1997
authors:
  item: Zehr JP
  item: Harris D
  item: Dominic B
  item: Salerno J

The first glimpse of a complex of nitrogenase component proteins by solution X-ray scattering: conformation of the electron transfer transition state complex of Klebsiella pneumoniae nitrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9102457
journal: J Mol Biol
volume: 266
pages: 642-8
published year: 1997
authors:
  item: Grossman JG
  item: Hasnain SS
  item: Yousafzai FK
  item: Smith BE
  item: Eady RR

Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
medline id: 97305952
references: http://www.ncbi.nlm.nih.gov/pubmed/9163420
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07328
references: P07329
journal: Nature
volume: 387
pages: 370-6
published year: 1997
authors:
  item: Schindelin H
  item: Kisker C
  item: Schlessman JL
  item: Howard JB
  item: Rees DC

Catalytic and biophysical properties of a nitrogenase Apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9730834
journal: Biochemistry
volume: 37
pages: 12611-23
published year: 1998
authors:
  item: Christiansen J
  item: Goodwin PJ
  item: Lanzilotta WN
  item: Seefeldt LC
  item: Dean DR

Evidence for coupled electron and proton transfer in the [8Fe-7S] cluster of nitrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9698385
journal: Biochemistry
volume: 37
pages: 11376-84
published year: 1998
authors:
  item: Lanzilotta WN
  item: Christiansen J
  item: Dean DR
  item: Seefeldt LC

Electron transfer in nitrogenase analyzed by Marcus theory: evidence for gating by MgATP.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9425061
journal: Biochemistry
volume: 37
pages: 399-407
published year: 1998
authors:
  item: Lanzilotta WN
  item: Parker VD
  item: Seefeldt LC

Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9710250
journal: FEBS Lett
volume: 432
pages: 55-8
published year: 1998
authors:
  item: Spee JH
  item: Arendsen AF
  item: Wassink H
  item: Marritt SJ
  item: Hagen WR
  item: Haaker H

An all-ferrous state of the Fe protein of nitrogenase. Interaction with nucleotides and electron transfer to the MoFe protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9756863
journal: J Biol Chem
volume: 273
pages: 26330-7
published year: 1998
authors:
  item: Angove HC
  item: Yoo SJ
  item: Munck E
  item: Burgess BK

The role of methionine 156 in cross-subunit nucleotide interactions in the iron protein of nitrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9792679
journal: J Biol Chem
volume: 273
pages: 29678-85
published year: 1998
authors:
  item: Bursey EH
  item: Burgess BK

Characterization of a variant iron protein of nitrogenase that is impaired in its ability to adopt the MgATP-induced conformational change.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9642255
journal: J Biol Chem
volume: 273
pages: 16927-34
published year: 1998
authors:
  item: Bursey EH
  item: Burgess BK

Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9677296
journal: J Mol Biol
volume: 280
pages: 669-85
published year: 1998
authors:
  item: Schlessman JL
  item: Woo D
  item: Joshua-Tor L
  item: Howard JB
  item: Rees DC

Nitrogenase of Azotobacter vinelandii: kinetic analysis of the Fe protein redox cycle.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9860849
journal: Biochemistry
volume: 37
pages: 17345-54
published year: 1998
authors:
  item: Duyvis MG
  item: Wassink H
  item: Haaker H

MgATP-independent hydrogen evolution catalysed by nitrogenase: an explanation for the missing electron(s) in the MgADP-AlF4 transition-state complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10215587
journal: Biochem J
volume: 339
pages: 511-5
published year: 1999
authors:
  item: Yousafzai FK
  item: Eady RR

Spectroscopic evidence for changes in the redox state of the nitrogenase P-cluster during turnover.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10231529
journal: Biochemistry
volume: 38
pages: 5779-85
published year: 1999
authors:
  item: Chan JM
  item: Christiansen J
  item: Dean DR
  item: Seefeldt LC

Evidence that MgATP accelerates primary electron transfer in a Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein nitrogenase tight complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10364195
journal: J Biol Chem
volume: 274
pages: 17593-8
published year: 1999
authors:
  item: Chan JM
  item: Ryle MJ
  item: Seefeldt LC

In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10391920
journal: J Biol Chem
volume: 274
pages: 19778-84
published year: 1999
authors:
  item: Rangaraj P
  item: Ryle MJ
  item: Lanzilotta WN
  item: Ludden PW
  item: Shah VK

New insights into structure-function relationships in nitrogenase: A 1.6 A resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10525412
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Mol Biol
volume: 292
pages: 871-91
published year: 1999
authors:
  item: Mayer SM
  item: Lawson DM
  item: Gormal CA
  item: Roe SM
  item: Smith BE

Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10852721
journal: Biochemistry
volume: 39
pages: 7221-8
published year: 2000
authors:
  item: Chan JM
  item: Wu W
  item: Dean DR
  item: Seefeldt LC

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00199#66
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10985789
journal: Biochemistry
volume: 39
pages: 11434-40
published year: 2000
authors:
  item: Clarke TA
  item: Maritano S
  item: Eady RR
title: Formation of a tight 1:1 complex of Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein: evidence for long-range interactions between the Fe protein binding sites during catalytic hydrogen evolution.

Mechanistic interpretation of the dilution effect for Azotobacter vinelandii and Clostridium pasteurianum nitrogenase catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11087939
journal: Biochim Biophys Acta
volume: 1543
pages: 36-46
published year: 2000
authors:
  item: Johnson JL
  item: Nyborg AC
  item: Wilson PE
  item: Tolley AM
  item: Nordmeyer FR
  item: Watt GD

Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
medline id: 20552920
references: http://www.ncbi.nlm.nih.gov/pubmed/11101289
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00459
journal: Biochemistry
volume: 39
pages: 14745-52
published year: 2000
authors:
  item: Jang SB
  item: Seefeldt LC
  item: Peters JW

Modulating the midpoint potential of the [4Fe-4S] cluster of the nitrogenase Fe protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10651628
journal: Biochemistry
volume: 39
pages: 641-8
published year: 2000
authors:
  item: Jang SB
  item: Seefeldt LC
  item: Peters JW

Analysis of steady state Fe and MoFe protein interactions during nitrogenase catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11087938
journal: Biochim Biophys Acta
volume: 1543
pages: 24-35
published year: 2000
authors:
  item: Johnson JL
  item: Nyborg AC
  item: Wilson PE
  item: Tolley AM
  item: Nordmeyer FR
  item: Watt GD

Nitrogenase: standing at the crossroads.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11006545
journal: Curr Opin Chem Biol
volume: 4
pages: 559-66
published year: 2000
authors:
  item: Rees DC
  item: Howard JB

Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10837496
journal: J Biol Chem
volume: 275
pages: 17631-8
published year: 2000
authors:
  item: Ribbe MW
  item: Bursey EH
  item: Burgess BK

Controlled protonation of iron-molybdenum cofactor by nitrogenase: a structural and theoretical analysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11311117
journal: Biochem J
volume: 355
pages: 569-76
published year: 2001
authors:
  item: Durrant MC

Interaction of acetylene and cyanide with the resting state of nitrogenase alpha-96-substituted MoFe proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11705370
journal: Biochemistry
volume: 40
pages: 13816-25
published year: 2001
authors:
  item: Benton PM
  item: Mayer SM
  item: Shao J
  item: Hoffman BM
  item: Dean DR
  item: Seefeldt LC

MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
medline id: 21093028
references: http://www.ncbi.nlm.nih.gov/pubmed/11170380
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07328
references: P07329
journal: Biochemistry
volume: 40
pages: 641-50
published year: 2001
authors:
  item: Chiu H
  item: Peters JW
  item: Lanzilotta WN
  item: Ryle MJ
  item: Seefeldt LC
  item: Howard JB
  item: Rees DC

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00199#76
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11258953
journal: Biochemistry
volume: 40
pages: 3333-9
published year: 2001
authors:
  item: Fisher K
  item: Newton WE
  item: Lowe DJ
title: Electron paramagnetic resonance analysis of different Azotobacter vinelandii nitrogenase MoFe-protein conformations generated during enzyme turnover: evidence for S = 3/2 spin states from reduced MoFe-protein intermediates.

Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11327812
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 40
pages: 1540-9
published year: 2001
authors:
  item: Sorlie M
  item: Christiansen J
  item: Lemon BJ
  item: Peters JW
  item: Dean DR
  item: Hales BJ

FeMo cofactor of nitrogenase: a density functional study of states M(N), M(OX), M(R), and M(I).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11734043
journal: J Am Chem Soc
volume: 123
pages: 12392-410
published year: 2001
authors:
  item: Lovell T
  item: Li J
  item: Liu T
  item: Case DA
  item: Noodleman L

Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 21093029
references: http://www.ncbi.nlm.nih.gov/pubmed/11170381
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00459
journal: Biochemistry
volume: 40
pages: 651-6
published year: 2001
authors:
  item: Strop P
  item: Takahara PM
  item: Chiu H
  item: Angove HC
  item: Burgess BK
  item: Rees DC

Great metalloclusters in enzymology.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12045096
journal: Annu Rev Biochem
volume: 71
pages: 221-46
published year: 2002
authors:
  item: Rees DC

Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12501184
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 41
pages: 15557-65
published year: 2002
authors:
  item: Schmid B
  item: Einsle O
  item: Chiu HJ
  item: Willing A
  item: Yoshida M
  item: Howard JB
  item: Rees DC

Metal substitution in the active site of nitrogenase MFe(7)S(9) (M = Mo(4+), V(3+), Fe(3+)).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12401079
journal: Inorg Chem
volume: 41
pages: 5744-53
published year: 2002
authors:
  item: Lovell T
  item: Torres RA
  item: Han WG
  item: Liu T
  item: Case DA
  item: Noodleman L

Synthesis and characterization of sulfur-voided cubanes. Structural analogues for the MoFe(3)S(3) subunit in the nitrogenase cofactor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11782173
journal: J Am Chem Soc
volume: 124
pages: 216-24
published year: 2002
authors:
  item: Coucouvanis D
  item: Han J
  item: Moon N

Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco).
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12133839
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Chem
volume: 277
pages: 35263-6
published year: 2002
authors:
  item: Mayer SM
  item: Gormal CA
  item: Smith BE
  item: Lawson DM

Accumulation of 99Mo-containing iron-molybdenum cofactor precursors of nitrogenase on NifNE, NifH, and NifX of Azotobacter vinelandii.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12176981
journal: J Biol Chem
volume: 277
pages: 40106-11
published year: 2002
authors:
  item: Rangaraj P
  item: Ludden PW

Molybdenum nitrogenases: a crystallographic and mechanistic view.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11913144
journal: Met Ions Biol Syst
volume: 39
pages: 75-119
published year: 2002
authors:
  item: Lawson DM
  item: Smith BE

Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS)
medline id: 22204524
references: http://www.ncbi.nlm.nih.gov/pubmed/12215645
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07328
references: P07329
journal: Science
volume: 297
pages: 1696-700
published year: 2002
authors:
  item: Einsle O
  item: Tezcan FA
  item: Andrade SL
  item: Schmid B
  item: Yoshida M
  item: Howard JB
  item: Rees DC

Structure of a cofactor-deficient nitrogenase MoFe protein.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
medline id: 21948294
references: http://www.ncbi.nlm.nih.gov/pubmed/11951047
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07328
references: P07329
journal: Science
volume: 296
pages: 352-6
published year: 2002
authors:
  item: Schmid B
  item: Ribbe MW
  item: Einsle O
  item: Yoshida M
  item: Thomas LM
  item: Dean DR
  item: Rees DC
  item: Burgess BK

Electron-transfer chemistry of the iron-molybdenum cofactor of nitrogenase: delocalized and localized reduced states of FeMoco which allow binding of carbon monoxide to iron and molybdenum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12506366
journal: Chemistry
volume: 9
pages: 76-87
published year: 2003
authors:
  item: Pickett CJ
  item: Vincent KA
  item: Ibrahim SK
  item: Gormal CA
  item: Smith BE
  item: Best SP

Comparison of iron-molybdenum cofactor-deficient nitrogenase MoFe proteins by X-ray absorption spectroscopy: implications for P-cluster biosynthesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15102840
journal: J Biol Chem
volume: 279
pages: 28276-82
published year: 2004
authors:
  item: Corbett MC
  item: Hu Y
  item: Naderi F
  item: Ribbe MW
  item: Hedman B
  item: Hodgson KO

Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15549494
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Inorg Chem
volume: 9
pages: 1028-33
published year: 2004
authors:
  item: Jang SB
  item: Jeong MS
  item: Seefeldt LC
  item: Peters JW

A conformational mimic of the MgATP-bound "on state" of the nitrogenase iron protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14967020
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 43
pages: 1787-97
published year: 2004
authors:
  item: Sen S
  item: Igarashi R
  item: Smith A
  item: Johnson MK
  item: Seefeldt LC
  item: Peters JW

Structural basis for the changes in redox potential in the nitrogenase Phe135Trp Fe protein with MgADP Bound.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15650336
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Mol Cells
volume: 18
pages: 374-82
published year: 2004
authors:
  item: Jeong MS
  item: Jang SB

Nitrogenase complexes: multiple docking sites for a nucleotide switch protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16123301
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Science
volume: 309
pages: 1377-80
published year: 2005
authors:
  item: Tezcan FA
  item: Kaiser JT
  item: Mustafi D
  item: Walton MY
  item: Howard JB
  item: Rees DC

Insights into the role of nucleotide-dependent conformational change in nitrogenase catalysis: Structural characterization of the nitrogenase Fe protein Leu127 deletion variant with bound MgATP.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16616373
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Inorg Biochem
volume: 100
pages: 1041-52
published year: 2006
authors:
  item: Sen S
  item: Krishnakumar A
  item: McClead J
  item: Johnson MK
  item: Seefeldt LC
  item: Szilagyi RK
  item: Peters JW

Analogue
compound: [8Fe-7S](P cluster)
pdb: 1mioB01
ligand het code: CLP

Analogue
compound: [8Fe-7S](P cluster)
pdb: 1mioD01
ligand het code: CLP

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 12
reference section: Scheme 1, Scheme 2, Scheme 3

ReferenceForCatalyticMechanism
reference index: 14
reference section: p.1680-1681

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reference index: 16
reference section: p.1657-1658

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.994

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig.9, p.347-349

ReferenceForCatalyticMechanism
reference index: 20
reference section: p.7112-7113

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig.2, Fig.3, p.794

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reference index: 33
reference section: p.27012-27013

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reference index: 35
reference section: p.10722

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reference section: p.13115-13117

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reference index: 40
reference section: p.16774-16775

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reference index: 41
reference section: p.9431-9432

ReferenceForCatalyticMechanism
reference index: 42
reference section: p.15660-15661

ReferenceForCatalyticMechanism
reference index: 46
reference section: Scheme 1, p.12981-12982

ReferenceForCatalyticMechanism
reference index: 47
reference section: Fig.2, Fig.4

ReferenceForCatalyticMechanism
reference index: 50
reference section: p.374-375

ReferenceForCatalyticMechanism
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reference section: p.11381-11383

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reference index: 53
reference section: p.404-406

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reference index: 64
reference section: p.881-886

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reference index: 68
reference section: p.14750-14751

ReferenceForCatalyticMechanism
reference index: 71
reference section: p.563-564

ReferenceForCatalyticMechanism
reference index: 73
reference section: Scheme 1, Scheme 2, Fig.3, Fig.4, p.571-575

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reference index: 74
reference section: p.13824

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reference section: p.648-650

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reference section: Fig.6

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reference section: Fig.7, Fig.8

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reference section: Fig.5, p.1698-1699

ReferenceForCatalyticMechanism
reference index: 89
reference section: Scheme 1, Scheme 2, Scheme 3, Scheme 4

ReferenceForCatalyticMechanism
reference index: 91
reference section: p.1032-1033

ReferenceForCatalyticMechanism
reference index: 93
reference section: p.380-381

ReferenceForCatalyticMechanism
reference index: 94
reference section: Fig.3

ReferenceForCatalyticMechanism
reference index: 95
reference section: Fig.8, p.1048-1051