M00042
type: Enzyme
rlcp: p10500
rlcp: p10510
rlcp: p10700
rlcp: p10750
rlcp: p10610
cath: Ubiquitin-like (UB roll)
cath: Helix Hairpins
cath: Alpha-Beta Plaits
cath: Rossmann fold
cath: Fe-only Hydrogenase (Larger Subunit); Chain L, domain 3
ec: https://purl.uniprot.org/enzyme/1.12.7.2
uniprot: P29166
kegg enzyme: ferredoxin hydrogenase
kegg enzyme: H2 oxidizing hydrogenase
kegg pathway: Glyoxylate and dicarboxylate metabolism
kegg pathway: Methane metabolism
kegg cofactor: [2Fe-2S]
kegg cofactor: [4Fe-4S]
kegg cofactor: [4Fe-4S]--diiron/2S/5CO(H-cluster)
kegg substrate: Reduced ferredoxin
kegg substrate: H+
kegg product: H2
kegg product: Oxidized ferredoxin
pdb: 1c4aA01
pdb: 1c4cA01
pdb: 1fehA01
pdb: 1c4aA02
pdb: 1c4cA02
pdb: 1fehA02
pdb: 1c4aA03
pdb: 1c4cA03
pdb: 1fehA03
pdb: 1c4aA04
pdb: 1c4cA04
pdb: 1fehA04
pdb: 1c4aA05
pdb: 1c4cA05
pdb: 1fehA05
active site residues resources: Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum.
active site residues resources: Hydrogenase sophistication.
active site residues resources: P29166
references: Purification and properties of the H2-oxidizing (uptake) hydrogenase of the N2-fixing anaerobe Clostridium pasteurianum W5.
references: The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I.
references: Mossbauer and electron nuclear double resonance study of oxidized bidirectional hydrogenase from Clostridium pasteurianum W5.
references: On the novel H2-activating iron-sulfur center of the "Fe-only" hydrogenases.
references: Mossbauer study of Clostridium pasteurianum hydrogenase II. Evidence for a novel three-iron cluster.
references: X-ray-absorption-spectroscopic evidence for a novel iron cluster in hydrogenase II from Clostridium pasteurianum.
references: Immunological relationship among hydrogenases.
references: Electron paramagnetic resonance studies of the low temperature photolytic behavior of oxidized hydrogenase I from Clostridium pasteurianum.
references: Magnetic circular dichroism and electron paramagnetic resonance studies of hydrogenases I and II from Clostridium pasteurianum.
references: Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum.
references: The structure and mechanism of iron-hydrogenases.
references: Primary structure of hydrogenase I from Clostridium pasteurianum.
references: Resonance Raman studies of iron-only hydrogenases.
references: Heterologous biosynthesis and characterization of the [2Fe-2S]-containing N-terminal domain of Clostridium pasteurianum hydrogenase.
references: Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli.
references: Biological hydrogen production: not so elementary.
references: X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
references: Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum.
references: Structure and mechanism of iron-only hydrogenases.
references: Hydrogenase sophistication.
references: Reversible carbon monoxide binding and inhibition at the active site of the Fe-only hydrogenase.
references: A novel FeS cluster in Fe-only hydrogenases.
references: A capable bridging ligand for Fe-only hydrogenase: density functional calculations of a low-energy route for heterolytic cleavage and formation of dihydrogen.
references: Coordination sphere flexibility of active-site models for Fe-only hydrogenase: studies in intra- and intermolecular diatomic ligand exchange.
references: Infrared studies of the CO-inhibited form of the Fe-only hydrogenase from Clostridium pasteurianum I: examination of its light sensitivity at cryogenic temperatures.
references: Hydrogenases: hydrogen-activating enzymes.
references: DFT investigation of structural, electronic, and catalytic properties of diiron complexes related to the [2Fe](H) subcluster of Fe-only hydrogenases.
references: Fe-only hydrogenases: structure, function and evolution.
references: Surprising cofactors in metalloenzymes.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/M00042#30
references: The organometallic active site of [Fe]hydrogenase: models and entatic states.
references: Hydrogenases: active site puzzles and progress.
references: Enzymatic mechanism of Fe-only hydrogenase: density functional study on H-H making/breaking at the diiron cluster with concerted proton and electron transfers.
references: A semi-empirical molecular orbital scheme to study electron transfer in iron-sulphur proteins.
references: Combined spectroscopic/computational study of binuclear Fe(I)-Fe(I) complexes: implications for the fully-reduced active-site cluster of Fe-only hydrogenases.
references: Synthetic chemistry: making a natural fuel cell.
references: Synthesis of the H-cluster framework of iron-only hydrogenase.
comment: This enzyme belongs to Fe-only hydrogenases. This enzyme is homologous to [Fe] hydrogenase (or DdH) (M00012 in EzCatDB). iomethyl)amine and 5 cyanide or carbon monoxide molecules. Although this enzyme is homologous to DdH (M00012), the direction of electron transfer is opposite to the counpterpart enzyme, DdH (see M00012). This enzyme binds five cofactors, a 2FE-2S cluster, three 4Fe-4S clusters, and one H cluster. The H cluster is composed of 4Fe-4S cluster, diiron (2Fe) subcluster, bridged via a thiolate of Cys503. The diiron subcluster is liganded by 2 sulfur atoms, 1 water, and 5 cyanide or carbon monoxide molecules. According to the literature [16], this enzyme catalyzes the following reactions: (A) Electron transfer from ferredoxin to the 2Fe-2S cluster: (A') Electron transfer from ferredoxin to the 4Fe-4S cluster-1: (B) Electron transfer from the 2Fe-2S cluster to the 4Fe-4S cluster-2: (B') Electron transfer from the 4Fe-4S cluster-1 to the 4Fe-4S cluster-2: (C) Electron transfer from the 4Fe-4S cluster-2 to the 4Fe-4S cluster-3: (D) Electron transfer from the 4Fe-4S cluster-3 to the H cluster: (E) Hydrogenation (H2 production from 2 H+ ions) at H cluster: The reactions proceeds as follows (see [17]): (A') Electron transfer from ferredoxin to the 4Fe-4S cluster-1: (A'1) Indirect transfer from 2Fe-2S of ferredoxin through Cys98 bound to 4Fe-4S cluster-1. (B) Electron transfer from the 2Fe-2S cluster to the 4Fe-4S cluster-2: (B1) Indirect transfer from Cys34 bound to 2Fe-2S to Cys150 bound to 4Fe-4S cluster-2. (B') Electron transfer from the 4Fe-4S cluster-1 to the 4Fe-4S cluster-2: (B'1) Indirect transfer from His94 bound to 4Fe-4S cluster-1 to either sulfur of the 4Fe-4S cluster-2 or Cys147 through Val202. (C) Electron transfer from the 4Fe-4S cluster-2 to the 4Fe-4S cluster-3: (C1) Indirect transfer from Cys153 bound to 4Fe-4S cluster-2 to Cys196 bound to 4Fe-4S cluster-3 (probably through Met166). (D) Electron transfer from the 4Fe-4S cluster-3 to the H clu…

Ubiquitin-like (UB roll)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.10.20.30
catalytic domain: index.html

Helix Hairpins
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.287.430
catalytic domain: index.html

Alpha-Beta Plaits
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.70.20
catalytic domain: index.html

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1780
catalytic domain: index.html

Fe-only Hydrogenase (Larger Subunit); Chain L, domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.950.10
catalytic domain: index.html

Glyoxylate and dicarboxylate metabolism
type: KeggPathway
references: KEGG:MAP00630

Methane metabolism
type: KeggPathway
references: KEGG:MAP00680

[2Fe-2S]
type: KeggCofactor
references: KEGG:L00023
compound type: heavy metal
compound type: sulfide group
references: CHEBI:33739

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

[4Fe-4S]--diiron/2S/5CO(H-cluster)
type: KeggCofactor
references: KEGG:L00029
compound type: heavy metal
compound type: sulfide group

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
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H2
type: KeggProduct
references: KEGG:C00282
compound type: others
references: CHEBI:18276
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

1c4aA01
type: Pdb
references: 1c4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4a
catalytic residue: CYS 34
cofactor binding residue: CYS 34;CYS 46;CYS 49;CYS 62(2Fe-2S cluster)

1c4cA01
type: Pdb
references: 1c4c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4c
catalytic residue: CYS 34
cofactor binding residue: CYS 34;CYS 46;CYS 49;CYS 62(2Fe-2S cluster)

1fehA01
type: Pdb
references: 1feh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1feh
catalytic residue: CYS 34
cofactor binding residue: CYS 34;CYS 46;CYS 49;CYS 62(2Fe-2S cluster)

1c4aA02
type: Pdb
references: 1c4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4a
catalytic residue: HIS 94;CYS 98
cofactor binding residue: HIS 94;CYS 98;CYS 101;CYS 107(4Fe-4S cluster-1)

1c4cA02
type: Pdb
references: 1c4c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4c
catalytic residue: HIS 94;CYS 98
cofactor binding residue: HIS 94;CYS 98;CYS 101;CYS 107(4Fe-4S cluster-1)

1fehA02
type: Pdb
references: 1feh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1feh
catalytic residue: HIS 94;CYS 98
cofactor binding residue: HIS 94;CYS 98;CYS 101;CYS 107(4Fe-4S cluster-1)

1c4aA03
type: Pdb
references: 1c4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4a
catalytic residue: CYS 147;CYS 150;CYS 153;MET 166;CYS 193;GLN 195;CYS 196;VAL 202
cofactor binding residue: CYS 147;CYS 150;CYS 153;CYS 200(4Fe-4S cluster-2);CYS 157;CYS 190;CYS 193;CYS 196(4Fe-4S cluster-3)

1c4cA03
type: Pdb
references: 1c4c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4c
catalytic residue: CYS 147;CYS 150;CYS 153;MET 166;CYS 193;GLN 195;CYS 196;VAL 202
cofactor binding residue: CYS 147;CYS 150;CYS 153;CYS 200(4Fe-4S cluster-2);CYS 157;CYS 190;CYS 193;CYS 196(4Fe-4S cluster-3)

1fehA03
type: Pdb
references: 1feh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1feh
catalytic residue: CYS 147;CYS 150;CYS 153;MET 166;CYS 193;GLN 195;CYS 196;VAL 202
cofactor binding residue: CYS 147;CYS 150;CYS 153;CYS 200(4Fe-4S cluster-2);CYS 157;CYS 190;CYS 193;CYS 196(4Fe-4S cluster-3)

1c4aA04
type: Pdb
references: 1c4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4a
catalytic residue: LYS 358
cofactor binding residue: CYS 355(4Fe-4S cluster-4 [H-cluster])

1c4cA04
type: Pdb
references: 1c4c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4c
catalytic residue: LYS 358
cofactor binding residue: CYS 355(4Fe-4S cluster-4 [H-cluster])

1fehA04
type: Pdb
references: 1feh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1feh
catalytic residue: LYS 358
cofactor binding residue: CYS 355(4Fe-4S cluster-4 [H-cluster])

1c4aA05
type: Pdb
references: 1c4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4a
catalytic residue: CYS 299;CYS 499
cofactor binding residue: CYS 300;CYS 499(4Fe-4S cluster-4 [H-cluster]);CYS 503(4Fe-4S cluster-4 & diiron [2Fe] subcluster [H-cluster])

1c4cA05
type: Pdb
references: 1c4c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4c
catalytic residue: CYS 299;CYS 499
cofactor binding residue: CYS 300;CYS 499(4Fe-4S cluster-4 [H-cluster]);CYS 503(4Fe-4S cluster-4 & diiron [2Fe] subcluster [H-cluster])

1fehA05
type: Pdb
references: 1feh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1feh
catalytic residue: CYS 299;CYS 499
cofactor binding residue: CYS 300;CYS 499(4Fe-4S cluster-4 [H-cluster]);CYS 503(4Fe-4S cluster-4 & diiron [2Fe] subcluster [H-cluster])

Purification and properties of the H2-oxidizing (uptake) hydrogenase of the N2-fixing anaerobe Clostridium pasteurianum W5.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6331453
journal: Biochem Biophys Res Commun
volume: 122
pages: 9-16
published year: 1984
authors:
  item: Chen JS
  item: Blanchard DK

The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6327705
journal: J Biol Chem
volume: 259
pages: 7045-55
published year: 1984
authors:
  item: Adams MW
  item: Mortenson LE

Mossbauer and electron nuclear double resonance study of oxidized bidirectional hydrogenase from Clostridium pasteurianum W5.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6094552
journal: J Biol Chem
volume: 259
pages: 14328-31
published year: 1984
authors:
  item: Wang G
  item: Benecky MJ
  item: Huynh BH
  item: Cline JF
  item: Adams MW
  item: Mortenson LE
  item: Hoffman BM
  item: Munck E

On the novel H2-activating iron-sulfur center of the "Fe-only" hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3015247
journal: Biochimie
volume: 68
pages: 35-42
published year: 1986
authors:
  item: Adams MW
  item: Johnson MK
  item: Zambrano IC
  item: Mortenson LE

Mossbauer study of Clostridium pasteurianum hydrogenase II. Evidence for a novel three-iron cluster.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3025213
journal: J Biol Chem
volume: 262
pages: 38-41
published year: 1987
authors:
  item: Rusnak FM
  item: Adams MW
  item: Mortenson LE
  item: Munck E

X-ray-absorption-spectroscopic evidence for a novel iron cluster in hydrogenase II from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2655584
journal: Biochem J
volume: 259
pages: 597-600
published year: 1989
authors:
  item: George GN
  item: Prince RC
  item: Stokley KE
  item: Adams MW
  item: Stockley KE

Immunological relationship among hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2464579
journal: J Bacteriol
volume: 171
pages: 430-5
published year: 1989
authors:
  item: Kovacs KL
  item: Seefeldt LC
  item: Tigyi G
  item: Doyle CM
  item: Mortenson LE
  item: Arp DJ

Electron paramagnetic resonance studies of the low temperature photolytic behavior of oxidized hydrogenase I from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2538440
journal: J Biol Chem
volume: 264
pages: 4342-8
published year: 1989
authors:
  item: Kowal AT
  item: Adams MW
  item: Johnson MK

Magnetic circular dichroism and electron paramagnetic resonance studies of hydrogenases I and II from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2556390
journal: J Biol Chem
volume: 264
pages: 20974-83
published year: 1989
authors:
  item: Zambrano IC
  item: Kowal AT
  item: Mortenson LE
  item: Adams MW
  item: Johnson MK

Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2544883
journal: Proc Natl Acad Sci U S A
volume: 86
pages: 4932-6
published year: 1989
authors:
  item: Adams MW
  item: Eccleston E
  item: Howard JB

The structure and mechanism of iron-hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2173950
journal: Biochim Biophys Acta
volume: 1020
pages: 115-45
published year: 1990
authors:
  item: Adams MW

Primary structure of hydrogenase I from Clostridium pasteurianum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1911757
journal: Biochemistry
volume: 30
pages: 9697-704
published year: 1991
authors:
  item: Meyer J
  item: Gagnon J

Resonance Raman studies of iron-only hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8490025
journal: Biochemistry
volume: 32
pages: 4813-9
published year: 1993
authors:
  item: Fu W
  item: Drozdzewski PM
  item: Morgan TV
  item: Mortenson LE
  item: Juszczak A
  item: Adams MW
  item: He SH
  item: Peck HD Jr
  item: DerVartanian DV
  item: LeGall J
  item: et al

Heterologous biosynthesis and characterization of the [2Fe-2S]-containing N-terminal domain of Clostridium pasteurianum hydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9843404
journal: Biochemistry
volume: 37
pages: 15974-80
published year: 1998
authors:
  item: Atta M
  item: Lafferty ME
  item: Johnson MK
  item: Gaillard J
  item: Meyer J

Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9485416
journal: Biochemistry
volume: 37
pages: 2660-5
published year: 1998
authors:
  item: De Luca G
  item: Asso M
  item: Belaich JP
  item: Dermoun Z

Biological hydrogen production: not so elementary.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9874636
journal: Science
volume: 282
pages: 1842-3
published year: 1998
authors:
  item: Adams MW
  item: Stiefel EI

X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
medline id: 99055388
references: http://www.ncbi.nlm.nih.gov/pubmed/9836629
journal: Science
volume: 282
pages: 1853-8
published year: 1998
authors:
  item: Peters JW
  item: Lanzilotta WN
  item: Lemon BJ
  item: Seefeldt LC
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P29166

Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
medline id: 99459241
references: http://www.ncbi.nlm.nih.gov/pubmed/10529166
journal: Biochemistry
volume: 38
pages: 12969-73
published year: 1999
authors:
  item: Lemon BJ
  item: Peters JW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P29166

Structure and mechanism of iron-only hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10607666
journal: Curr Opin Struct Biol
volume: 9
pages: 670-6
published year: 1999
authors:
  item: Peters JW

Hydrogenase sophistication.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9930693
journal: Nature
volume: 397
pages: 214-5
published year: 1999
authors:
  item: Cammack R

Reversible carbon monoxide binding and inhibition at the active site of the Fe-only hydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10858294
journal: Biochemistry
volume: 39
pages: 7455-60
published year: 2000
authors:
  item: Bennett B
  item: Lemon BJ
  item: Peters JW

A novel FeS cluster in Fe-only hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10694885
journal: Trends Biochem Sci
volume: 25
pages: 138-43
published year: 2000
authors:
  item: Nicolet Y
  item: Lemon BJ
  item: Fontecilla-Camps JC
  item: Peters JW

A capable bridging ligand for Fe-only hydrogenase: density functional calculations of a low-energy route for heterolytic cleavage and formation of dihydrogen.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11457119
journal: J Am Chem Soc
volume: 123
pages: 3828-9
published year: 2001
authors:
  item: Fan HJ
  item: Hall MB

Coordination sphere flexibility of active-site models for Fe-only hydrogenase: studies in intra- and intermolecular diatomic ligand exchange.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11457062
journal: J Am Chem Soc
volume: 123
pages: 3268-78
published year: 2001
authors:
  item: Lyon EJ
  item: Georgakaki IP
  item: Reibenspies JH
  item: Darensbourg MY

Infrared studies of the CO-inhibited form of the Fe-only hydrogenase from Clostridium pasteurianum I: examination of its light sensitivity at cryogenic temperatures.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11827551
journal: Biochemistry
volume: 41
pages: 2036-43
published year: 2002
authors:
  item: Chen Z
  item: Lemon BJ
  item: Huang S
  item: Swartz DJ
  item: Peters JW
  item: Bagley KA

Hydrogenases: hydrogen-activating enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11921392
journal: Chembiochem
volume: 3
pages: 153-60
published year: 2002
authors:
  item: Frey M

DFT investigation of structural, electronic, and catalytic properties of diiron complexes related to the [2Fe](H) subcluster of Fe-only hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11896710
journal: Inorg Chem
volume: 41
pages: 1421-9
published year: 2002
authors:
  item: Bruschi M
  item: Fantucci P
  item: De Gioia L

Fe-only hydrogenases: structure, function and evolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12121756
journal: J Inorg Biochem
volume: 91
pages: 1-8
published year: 2002
authors:
  item: Nicolet Y
  item: Cavazza C
  item: Fontecilla-Camps JC

Surprising cofactors in metalloenzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12727516
journal: Curr Opin Struct Biol
volume: 13
pages: 220-6
published year: 2003
authors:
  item: Drennan CL
  item: Peters JW

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00042#30
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12870970
journal: Inorg Chem
volume: 42
pages: 4773-81
published year: 2003
authors:
  item: Bruschi M
  item: Fantucci P
  item: De Gioia L
title: Density functional theory investigation of the active site of [Fe]-hydrogenases: effects of redox state and ligand characteristics on structural, electronic, and reactivity properties of complexes related to the [2Fe]H subcluster.

The organometallic active site of [Fe]hydrogenase: models and entatic states.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12642671
journal: Proc Natl Acad Sci U S A
volume: 100
pages: 3683-8
published year: 2003
authors:
  item: Darensbourg MY
  item: Lyon EJ
  item: Zhao X
  item: Georgakaki IP

Hydrogenases: active site puzzles and progress.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15062773
journal: Curr Opin Chem Biol
volume: 8
pages: 133-40
published year: 2004
authors:
  item: Armstrong FA

Enzymatic mechanism of Fe-only hydrogenase: density functional study on H-H making/breaking at the diiron cluster with concerted proton and electron transfers.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14753812
journal: Inorg Chem
volume: 43
pages: 923-30
published year: 2004
authors:
  item: Zhou T
  item: Mo Y
  item: Liu A
  item: Zhou Z
  item: Tsai KR

A semi-empirical molecular orbital scheme to study electron transfer in iron-sulphur proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15667253
journal: Biochem Soc Trans
volume: 33
pages: 20-1
published year: 2005
authors:
  item: Sundararajan M
  item: McNamara JP
  item: Mohr M
  item: Hillier IH
  item: Wang H

Combined spectroscopic/computational study of binuclear Fe(I)-Fe(I) complexes: implications for the fully-reduced active-site cluster of Fe-only hydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15762706
journal: Inorg Chem
volume: 44
pages: 1794-809
published year: 2005
authors:
  item: Fiedler AT
  item: Brunold TC

Synthetic chemistry: making a natural fuel cell.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15703733
journal: Nature
volume: 433
pages: 589-91
published year: 2005
authors:
  item: Darensbourg MY

Synthesis of the H-cluster framework of iron-only hydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15703741
journal: Nature
volume: 433
pages: 610-3
published year: 2005
authors:
  item: Tard C
  item: Liu X
  item: Ibrahim SK
  item: Bruschi M
  item: De Gioia L
  item: Davies SC
  item: Yang X
  item: Wang LS
  item: Sawers G
  item: Pickett CJ

H2 producing hydrogenase [ambiguous]
type: KeggEnzyme

bidirectional hydrogenase
type: KeggEnzyme

hydrogen-lyase [ambiguous]
type: KeggEnzyme

hydrogenase (ferredoxin)
type: KeggEnzyme

hydrogenase I
type: KeggEnzyme

hydrogenase II
type: KeggEnzyme

hydrogenlyase [ambiguous]
type: KeggEnzyme

uptake hydrogenase [ambiguous]
type: KeggEnzyme

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 16

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.1856-1857

ReferenceForCatalyticMechanism
reference index: 27
reference section: Scheme 1, p.1428

ReferenceForCatalyticMechanism
reference index: 30
reference section: Scheme 3, p.4780

ReferenceForCatalyticMechanism
reference index: 33
reference section: Fig.5, p.926-930
reference step: 6