M00039
type: Enzyme
cath: Ubiquitin-like (UB roll)
cath: DNA polymerase; domain 1
cath: Aldehyde Oxidoreductase; domain 3
cath: Aldehyde Oxidoreductase; domain 4
cath: Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
cath: Enolase-like; domain 1
cath: Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
ec: https://purl.uniprot.org/enzyme/1.2.99.2
csa: 1qj2
macie: M0107
uniprot: P19921
uniprot: P19919
uniprot: P19920
kegg enzyme: carbon-monoxide dehydrogenase (acceptor)
kegg pathway: Trinitrotoluene degradation
kegg pathway: Methane metabolism
kegg cofactor: [2Fe-2S]
kegg cofactor: Dinuclear [Cu-S-Mo(=O)OH] cluster
kegg cofactor: Molybdopterin cytosine dinucleotide
kegg cofactor: FAD
kegg substrate: CO
kegg substrate: H2O
kegg substrate: Acceptor
kegg product: CO2
kegg product: Reduced acceptor
pdb: 1n5wA01
pdb: 1n5wD01
pdb: 1n60A01
pdb: 1n60D01
pdb: 1n61A01
pdb: 1n61D01
pdb: 1n62A01
pdb: 1n62D01
pdb: 1n63A01
pdb: 1n63D01
pdb: 1qj2A01
pdb: 1qj2G01
pdb: 1zxiA01
pdb: 1zxiD01
pdb: 1n5wA02
pdb: 1n5wD02
pdb: 1n60A02
pdb: 1n60D02
pdb: 1n61A02
pdb: 1n61D02
pdb: 1n62A02
pdb: 1n62D02
pdb: 1n63A02
pdb: 1n63D02
pdb: 1qj2A02
pdb: 1qj2G02
pdb: 1zxiA02
pdb: 1zxiD02
pdb: 1n5wB01
pdb: 1n5wE01
pdb: 1n60B01
pdb: 1n60E01
pdb: 1n61B01
pdb: 1n61E01
pdb: 1n62B01
pdb: 1n62E01
pdb: 1n63B01
pdb: 1n63E01
pdb: 1qj2B01
pdb: 1qj2H01
pdb: 1zxiB01
pdb: 1zxiE01
pdb: 1n5wB02
pdb: 1n5wE02
pdb: 1n60B02
pdb: 1n60E02
pdb: 1n61B02
pdb: 1n61E02
pdb: 1n62B02
pdb: 1n62E02
pdb: 1n63B02
pdb: 1n63E02
pdb: 1qj2B02
pdb: 1qj2H02

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

DNA polymerase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.150.120
catalytic domain: index.html

Aldehyde Oxidoreductase; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.1170.50

Aldehyde Oxidoreductase; domain 4
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.365.10
catalytic domain: index.html

Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.43.10

Enolase-like; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.390.50

Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.465.10
catalytic domain: index.html

Trinitrotoluene degradation
type: KeggPathway
references: KEGG:MAP00633

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

Dinuclear [Cu-S-Mo(=O)OH] cluster
type: KeggCofactor
references: KEGG:C99999
compound type: heavy metal
compound type: sulfide group

Molybdopterin cytosine dinucleotide
type: KeggCofactor
references: KEGG:L00006
compound type: amide group
compound type: amine group
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide
compound type: sulfhydryl group
references: CHEBI:43955
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

FAD
type: KeggCofactor
references: KEGG:C00016
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide
references: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

CO
type: KeggSubstrate
references: KEGG:C00237
compound type: others
references: CHEBI:17245
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

Acceptor
type: KeggSubstrate
references: KEGG:C00028
compound type: others

CO2
type: KeggProduct
references: KEGG:C00011
compound type: others
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Reduced acceptor
type: KeggProduct
references: KEGG:C00030
compound type: others

1n5wA01
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n5wD01
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n60A01
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n60D01
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n61A01
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n61D01
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n62A01
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n62D01
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n63A01
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n63D01
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1qj2A01
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1qj2G01
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1zxiA01
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1zxiD01
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)

1n5wA02
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n5wD02
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n60A02
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n60D02
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n61A02
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n61D02
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n62A02
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n62D02
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n63A02
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n63D02
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1qj2A02
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1qj2G02
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1zxiA02
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1zxiD02
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)

1n5wB04
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n5wE04
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n60B04
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n60E04
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n61B04
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n61E04
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n62B04
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n62E04
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n63B04
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n63E04
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1qj2B04
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
catalytic residue: ;GLU 763
cofactor binding residue: EYS 388(Copper binding);GLU 763(Molybdenum binding)
modified residue: EYS 388(Selanylated)
main chain in catalysis: ARG 387

1qj2H04
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
catalytic residue: ;GLU 763
cofactor binding residue: EYS 388(Copper binding);GLU 763(Molybdenum binding)
modified residue: EYS 388(Selanylated)
main chain in catalysis: ARG 387

1zxiB04
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1zxiE04
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387

1n5wB05
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
catalytic residue: GLN 240

1n5wE05
type: Pdb
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w
catalytic residue: GLN 240

1n60B05
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
catalytic residue: GLN 240

1n60E05
type: Pdb
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60
catalytic residue: GLN 240

1n61B05
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
catalytic residue: GLN 240

1n61E05
type: Pdb
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61
catalytic residue: GLN 240

1n62B05
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
catalytic residue: GLN 240

1n62E05
type: Pdb
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62
catalytic residue: GLN 240

1n63B05
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
catalytic residue: GLN 240

1n63E05
type: Pdb
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63
catalytic residue: GLN 240

1qj2B05
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
catalytic residue: GLN 240

1qj2H05
type: Pdb
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2
catalytic residue: GLN 240

1zxiB05
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
catalytic residue: GLN 240

1zxiE05
type: Pdb
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi
catalytic residue: GLN 240

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
pdb: 1n60B04
ligand het code: OMO

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
pdb: 1n60E04
ligand het code: OMO

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
pdb: 1n62B04
ligand het code: CUB

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
pdb: 1n62E04
ligand het code: CUB

Analogue
compound: Molybdopterin cytosine dinucleotide
pdb: 1qj2B03
ligand het code: PCD

Analogue
compound: Molybdopterin cytosine dinucleotide
pdb: 1qj2H03
ligand het code: PCD

Analogue
compound: FAD
pdb: 1n5wC03
ligand het code: FAD

Analogue
compound: FAD
pdb: 1n5wF03
ligand het code: FAD

IntermediateAnalogue
pdb: 1n62B04
ligand het code: CUB

IntermediateAnalogue
pdb: 1n62E04
ligand het code: CUB

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.4, p.8887-8889

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.5, p.871-875

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.1224-1228

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.2, p.15974-15976

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig. 2, Fig. 6, Fig. 12, p.891-897

Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
medline id: 99362680
references: http://www.ncbi.nlm.nih.gov/pubmed/10430865
journal: Proc Natl Acad Sci U S A
volume: 96
pages: 8884-9
published year: 1999
authors:
  item: Dobbek H
  item: Gremer L
  item: Meyer O
  item: Huber R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P19919
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The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11076018
journal: Biol Chem
volume: 381
pages: 865-76
published year: 2000
authors:
  item: Meyer O
  item: Gremer L
  item: Ferner R
  item: Ferner M
  item: Dobbek H
  item: Gnida M
  item: Meyer-Klaucke W
  item: Huber R

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00039#3
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10636886
journal: J Biol Chem
volume: 275
pages: 1864-72
published year: 2000
authors:
  item: Gremer L
  item: Kellner S
  item: Dobbek H
  item: Huber R
  item: Meyer O
title: Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli.

The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10966817
journal: J Mol Biol
volume: 301
pages: 1221-35
published year: 2000
authors:
  item: Hanzelmann P
  item: Dobbek H
  item: Gremer L
  item: Huber R
  item: Meyer O

Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).
medline id: 22364130
references: http://www.ncbi.nlm.nih.gov/pubmed/12475995
journal: Proc Natl Acad Sci U S A
volume: 99
pages: 15971-6
published year: 2002
authors:
  item: Dobbek H
  item: Gremer L
  item: Kiefersauer R
  item: Huber R
  item: Meyer O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P19919
references: P19920
references: P19921

A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12515558
journal: Biochemistry
volume: 42
pages: 222-30
published year: 2003
authors:
  item: Gnida M
  item: Ferner R
  item: Gremer L
  item: Meyer O
  item: Meyer-Klaucke W

Quantum chemical modeling of CO oxidation by the active site of molybdenum CO dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15834924
journal: J Comput Chem
volume: 26
pages: 888-98
published year: 2005
authors:
  item: Siegbahn PE
  item: Shestakov AF

Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16091936
journal: J Biol Inorg Chem
volume: 10
pages: 518-28
published year: 2005
authors:
  item: Resch M
  item: Dobbek H
  item: Meyer O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

anaerobic carbon monoxide dehydrogenase
type: KeggEnzyme

carbon monoxide oxygenase
type: KeggEnzyme

carbon-monoxide dehydrogenase
type: KeggEnzyme

carbon-monoxide:(acceptor) oxidoreductase
type: KeggEnzyme