DB code: T00030

RLCP classification 10.22023.100.10525 : Electron transfer
10.23022.100.10580 : Electron transfer
10.22140.100.10551 : Electron transfer
CATH domain 1.10.645.10 : Cytochrome-c3 Hydrogenase; chain B Catalytic domain
3.40.50.700 : Rossmann fold Catalytic domain
4.10.480.10 : Cytochrome-c3 Hydrogenase; Chain A, domain 2 Catalytic domain
E.C. 1.12.2.1
CSA 1h2r
M-CSA 1h2r
MACiE M0126

CATH domain Related DB codes (homologues)
1.10.645.10 : Cytochrome-c3 Hydrogenase; chain B T00238
3.40.50.700 : Rossmann fold T00238
4.10.480.10 : Cytochrome-c3 Hydrogenase; Chain A, domain 2 T00238

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P21852 Periplasmic [NiFe] hydrogenase large subunit
NiFe hydrogenlyase large chain
EC 1.12.2.1
YP_002434695.1 (Protein)
NC_011769.1 (DNA/RNA sequence)
PF00374 (NiFeSe_Hases)
[Graphical View]
P18188 Periplasmic [NiFe] hydrogenase large subunit
EC 1.12.2.1
NiFe hydrogenlyase large chain
PF00374 (NiFeSe_Hases)
[Graphical View]
P12944 Periplasmic [NiFe] hydrogenase large subunit
EC 1.12.2.1
NiFe hydrogenlyase large chain
PF00374 (NiFeSe_Hases)
[Graphical View]
P18187 Periplasmic [NiFe] hydrogenase small subunit
EC 1.12.2.1
NiFe hydrogenlyase small chain
PF01058 (Oxidored_q6)
PF10518 (TAT_signal)
[Graphical View]
P12943 Periplasmic [NiFe] hydrogenase small subunit
EC 1.12.2.1
NiFe hydrogenlyase small chain
PF01058 (Oxidored_q6)
[Graphical View]
P21853 Periplasmic [NiFe] hydrogenase small subunit
EC 1.12.2.1
NiFe hydrogenlyase small chain
YP_002434696.1 (Protein)
NC_011769.1 (DNA/RNA sequence)
PF01058 (Oxidored_q6)
[Graphical View]

KEGG enzyme name
cytochrome-c3 hydrogenase
H2:ferricytochrome c3 oxidoreductase
cytochrome c3 reductase
cytochrome hydrogenase
hydrogenase [ambiguous]

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P18188 PHNL_DESFR 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. Heterodimer of a large and a small subunit. Periplasm. Binds 1 nickel ion per subunit.
P12944 PHNL_DESGI 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. Heterodimer of a large and a small subunit. Periplasm. Binds 1 nickel ion per subunit.
P21852 PHNL_DESVM 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. Heterodimer of a large and a small subunit. Periplasm. Nickel. Iron.
P18187 PHNS_DESFR 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. Heterodimer of a large and a small subunit. Periplasm. Binds 2 4Fe-4S clusters. Binds 1 3Fe-4S cluster.
P12943 PHNS_DESGI 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. Heterodimer of a large and a small subunit. Periplasm. Binds 2 4Fe-4S clusters. Binds 1 3Fe-4S cluster.
P21853 PHNS_DESVM 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. Heterodimer of a large and a small subunit. Periplasm. Binds 2 4Fe-4S clusters. Binds 1 3Fe-4S cluster.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id L00024 L00027 L00028 C00282 C02682 C00080 C02684
E.C. (peroxide bound)
(oxygen atom bound)
Compound [4Fe-4S] [3Fe-4S] Ni--Fe(CN)2(CO) H2 ferricytochrome c3 H+ ferrocytochrome c3 Transition-state Transition-state
Type heavy metal,sulfide group heavy metal,sulfide group heavy metal,others others aromatic ring (with nitrogen atoms),carbohydrate,heavy metal,peptide/protein,sulfide group others aromatic ring (with nitrogen atoms),carbohydrate,heavy metal,peptide/protein,sulfide group
ChEBI 33725
33725
47402
47402
18276
18276
15378
15378
PubChem 58838673
783
58838673
783
1038
1038
1frfL Unbound Unbound Analogue:_NI-Fe Unbound Unbound Unbound
1yqwQ Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:PER (Ni-SU status)
1yqwR Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:PER (Ni-SU status)
1yqwS Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:PER (Ni-SU status)
1yrqH Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound
1yrqI Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound
1yrqJ Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound
1yrqK Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound
1yrqM Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound
1yrqN Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound
1frvB Unbound Unbound Analogue:_NI-FEL Unbound Unbound Unbound
1frvD Unbound Unbound Analogue:_NI-FEL Unbound Unbound Unbound
1yq9H Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:PER (Ni-A status)
1yq9I Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:PER (Ni-A status)
2frvB Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:__O (Ni-B state)
2frvD Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:__O (Ni-B state)
2frvF Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:__O (Ni-B state)
2frvH Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:__O (Ni-B state)
2frvJ Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:__O (Ni-B state)
2frvL Unbound Unbound Bound:_NI-FCO Unbound Unbound Unbound Transition-state-bound:__O (Ni-B state)
1h2aL Unbound Unbound Analogue:NFE Unbound Unbound Unbound
1h2rL Unbound Unbound Analogue:NFE Unbound Unbound Unbound
1ubhL Unbound Unbound Analogue:FNE-CMO Unbound Unbound Unbound
1ubjL Unbound Unbound Analogue:FNE-CMO Unbound Unbound Unbound
1ubkL Unbound Unbound Analogue:FNE-CMO Unbound Unbound Unbound
1ublL Unbound Unbound Analogue:FNE-CMO Unbound Unbound Unbound
1ubmL Unbound Unbound Analogue:FNE Unbound Unbound Unbound
1uboL Unbound Unbound Analogue:FNE-CMO Unbound Unbound Unbound
1ubrL Unbound Unbound Analogue:FNE-CMO Unbound Unbound Unbound
1ubtL Unbound Unbound Analogue:FNE Unbound Unbound Unbound
1ubuL Unbound Unbound Analogue:FNE Unbound Unbound Unbound
1wuhL Unbound Unbound Analogue:NFC Unbound Unbound Unbound Transition-state-bound:NFC (Ni-A status)
1wuiL Unbound Unbound Analogue:NFC Unbound Unbound Unbound Transition-state-bound:NFC (Ni-A status)
1wujL Unbound Unbound Analogue:NFO Unbound Unbound Unbound Transition-state-bound:NFO (Ni-B status)
1wukL Unbound Unbound Analogue:NFO Unbound Unbound Unbound Transition-state-bound:NFO (oxidized status)
1wulL Unbound Unbound Bound:NFR Unbound Unbound Unbound
1frfS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yqwA01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yqwB01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yqwC01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yrqA01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yrqB01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yrqC01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yrqD01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yrqF01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yrqG01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1frvA01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1frvC01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yq9A01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1yq9B01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
2frvA01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
2frvC01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
2frvE01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
2frvG01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
2frvI01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
2frvS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1h2aS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1h2rS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ubhS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ubjS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ubkS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ublS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ubmS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1uboS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ubrS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ubtS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1ubuS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1wuhS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1wuiS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1wujS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1wukS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1wulS01 Bound:SF4 Unbound Unbound Unbound Unbound Unbound
1frfS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yqwA02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yqwB02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yqwC02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yrqA02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yrqB02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yrqC02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yrqD02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yrqF02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yrqG02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1frvA02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1frvC02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yq9A02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1yq9B02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
2frvA02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
2frvC02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
2frvE02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
2frvG02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
2frvI02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
2frvS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1h2aS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1h2rS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ubhS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ubjS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ubkS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ublS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ubmS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1uboS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ubrS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ubtS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1ubuS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1wuhS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1wuiS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1wujS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1wukS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound
1wulS02 Bound:SF4 Bound:F3S Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [31], [32], [35], [37], [39], [45], [47]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1frfL GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yqwQ GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yqwR GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yqwS GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yrqH GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yrqI GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yrqJ GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yrqK GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yrqM GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1yrqN GLU 25;CYS 543 CYS 75;CYS 546(Fe and Nickel);CYS 72;CYS 543(Nickel)
1frvB GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
1frvD GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
1yq9H GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
1yq9I GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
2frvB GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
2frvD GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
2frvF GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
2frvH GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
2frvJ GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
2frvL GLU 18;CYS 530 CYS 68;CYS 533(Fe and Nickel);CYS 65;CYS 530(Nickel)
1h2aL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1h2rL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ubhL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ubjL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ubkL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ublL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ubmL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1uboL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ubrL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ubtL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1ubuL GLU 34;CYS 546 CYS 84;CYS 549(Fe and Nickel);CYS 81;CYS 546(Nickel)
1wuhL GLU 34; CSO 84;CYS 549(Fe and Nickel);CYS 81;CSO 546(Nickel) CSO 84;CSO 546
1wuiL GLU 34; CSO 84;CYS 549(Fe and Nickel);CYS 81;CSO 546(Nickel) CSO 84;CSO 546
1wujL GLU 34; CYS 84;CYS 549(Fe and Nickel);CYS 81;CSO 546(Nickel) ;CSO 546
1wukL GLU 34; CYS 84;CYS 549(Fe and Nickel);CYS 81;CSO 546(Nickel) ;CSO 546
1wulL GLU 34; CYS 84;CYS 549(Fe and Nickel);CYS 81;CSO 546(Nickel) ;CSO 546
1frfS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yqwA01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yqwB01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yqwC01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yrqA01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yrqB01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yrqC01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yrqD01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yrqF01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1yrqG01 THR 18 CYS 17;CYS 20;CYS 114;CYS 147(4Fe-4S cluster-1)
1frvA01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
1frvC01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
1yq9A01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
1yq9B01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
2frvA01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
2frvC01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
2frvE01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
2frvG01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
2frvI01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
2frvS01 THR 18 CYS 17;CYS 20;CYS 112;CYS 148(4Fe-4S cluster-1)
1h2aS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1h2rS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ubhS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ubjS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ubkS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ublS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ubmS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1uboS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ubrS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ubtS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1ubuS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1wuhS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1wuiS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1wujS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1wukS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1wulS01 THR 18 CYS 17;CYS 20;CYS 114;CYS 150(4Fe-4S cluster-1)
1frfS02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yqwA02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yqwB02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yqwC02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yrqA02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yrqB02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yrqC02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yrqD02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yrqF02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1yrqG02 HIS 184;CYS 187;CYS 212;CYS 218(4Fe-4S cluster-2);CYS 227;CYS 245;CYS 248(3Fe-4S cluster)
1frvA02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
1frvC02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
1yq9A02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
1yq9B02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
2frvA02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
2frvC02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
2frvE02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
2frvG02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
2frvI02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
2frvS02 HIS 185;CYS 188;CYS 213;CYS 219(4Fe-4S cluster-2);CYS 228;CYS 246;CYS 249(3Fe-4S cluster)
1h2aS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1h2rS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ubhS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ubjS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ubkS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ublS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ubmS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1uboS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ubrS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ubtS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1ubuS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1wuhS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1wuiS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1wujS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1wukS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)
1wulS02 HIS 188;CYS 191;CYS 216;CYS 222(4Fe-4S cluster-2);CYS 231;CYS 249;CYS 252(3Fe-4S cluster)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[7]
p.987-988
[9]
Fig.5, Fig.9, Fig.10, p.14346-14348
[10]
p.825-828
[12]
Fig.5, p.582-585
[14]
Fig.7, p.12995-12996
[16]
Fig.4, p.7850-7854
[17]
Fig.2, p.664-665
[20]
p.1675-1677
[21]
p.399-400
[22]
p.11628-11630
[23]
p.298
[24]
p.3336-3337
[25]
Fig.3, p.553-554
[31]
Scheme 1, Fig.2, p.6202-6203
[32]
Scheme 1, p.5840 2
[33]
Table 1, p.469-472
[34]
p.457-458
[35]
p.71-73, p.77-80
[36]
p.156-157, p.158-159
[37]
Fig.4, p.4432-4434
[38]
Fig.7, p.11634-11635
[42]
Fig.8, p.92
[44]
Fig.2, p.134-138
[45]
p.10511-10513
[47]
Fig.1, p.641-642
[48]
Fig3., Fig.4, p.872-875
[50]
Fig.6, p.246-248
[51]
Fig.3, p.1637-1640

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Medline ID
PubMed ID 6096145
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Year 1984
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Pages 637-43
Authors Rieder R, Cammack R, Hall DO
Title Purification and properties of the soluble hydrogenase from Desulfovibrio desulfuricans (strain Norway 4).
Related PDB
Related UniProtKB
[2]
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Comments
Medline ID
PubMed ID 2987196
Journal J Biochem (Tokyo)
Year 1985
Volume 97
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Authors Yagi T, Kimura K, Inokuchi H
Title Analysis of the active center of hydrogenase from Desulfovibrio vulgaris Miyazaki by magnetic measurements.
Related PDB
Related UniProtKB
[3]
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Medline ID
PubMed ID 2154378
Journal Eur J Biochem
Year 1990
Volume 187
Pages 635-43
Authors Hatchikian CE, Traore AS, Fernandez VM, Cammack R
Title Characterization of the nickel-iron periplasmic hydrogenase from Desulfovibrio fructosovorans.
Related PDB
Related UniProtKB P18187 P18188
[4]
Resource
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Medline ID
PubMed ID 1316088
Journal Anal Chem
Year 1992
Volume 64
Pages 641-6
Authors Parpaleix T, Laval JM, Majda M, Bourdillon C
Title Potentiometric and voltammetric investigations of H2/H+ catalysis by periplasmic hydrogenase from Desulfovibrio gigas immobilized at the electrode surface in an amphiphilic bilayer assembly.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1558764
Journal FEMS Microbiol Rev
Year 1992
Volume 8
Pages 109-35
Authors Przybyla AE, Robbins J, Menon N, Peck HD Jr
Title Structure-function relationships among the nickel-containing hydrogenases.
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Related UniProtKB
[6]
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Comments
Medline ID
PubMed ID 8399280
Journal Biochim Biophys Acta
Year 1993
Volume 1144
Pages 302-8
Authors Franco R, Moura I, LeGall J, Peck HD Jr, Huynh BH, Moura JJ
Title Characterization of D. desulfuricans (ATCC 27774) [NiFe] hydrogenase EPR and redox properties of the native and the dihydrogen reacted states.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8223656
Journal Eur J Biochem
Year 1993
Volume 217
Pages 981-9
Authors Moreno C, Franco R, Moura I, Le Gall J, Moura JJ
Title Voltammetric studies of the catalytic electron-transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8501043
Journal J Bacteriol
Year 1993
Volume 175
Pages 3388-93
Authors Rousset M, Dermoun Z, Wall JD, Belaich JP
Title Analysis of the periplasmic [NiFe] hydrogenase transcription unit from Desulfovibrio fructosovorans.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7947844
Journal Biochemistry
Year 1994
Volume 33
Pages 14339-50
Authors Roberts LM, Lindahl PA
Title Analysis of oxidative titrations of Desulfovibrio gigas hydrogenase; implications for the catalytic mechanism.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8174562
Journal Eur J Biochem
Year 1994
Volume 221
Pages 821-9
Authors Verhagen MF, Wolbert RB, Hagen WR
Title Cytochrome c553 from Desulfovibrio vulgaris (Hildenborough). Electrochemical properties and electron transfer with hydrogenase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 7718585
Journal Biochemistry
Year 1995
Volume 34
Pages 4781-90
Authors Guigliarelli B, More C, Fournel A, Asso M, Hatchikian EC, Williams R, Cammack R, Bertrand P
Title Structural organization of the Ni and (4Fe-4S) centers in the active form of Desulfovibrio gigas hydrogenase. Analysis of the magnetic interactions by electron paramagnetic resonance spectroscopy.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS).
Medline ID
PubMed ID 7854413
Journal Nature
Year 1995
Volume 373
Pages 580-7
Authors Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M, Fontecilla-Camps JC
Title Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.
Related PDB 1frv
Related UniProtKB P12943 P12944
[13]
Resource
Comments
Medline ID
PubMed ID 8973216
Journal Biochemistry
Year 1996
Volume 35
Pages 16399-406
Authors Dole F, Medina M, More C, Cammack R, Bertrand P, Guigliarelli B
Title Spin-spin interactions between the Ni site and the [4Fe-4S] centers as a probe of light-induced structural changes in active Desulfovibrio gigas hydrogenase.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 1996
Volume 118
Pages 12989-96
Authors Volbeda A, Garcin E, Piras C, de Lacey A L, Fernandez VM, Hatchikian EC, Frey M, Fontecilla-Camps JC
Title Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands.
Related PDB 2frv
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 8605619
Journal Nat Struct Biol
Year 1996
Volume 3
Pages 213-7
Authors Collman JP
Title Coupling H2 to electron transfer.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9201928
Journal Biochemistry
Year 1997
Volume 36
Pages 7847-54
Authors Dole F, Fournel A, Magro V, Hatchikian EC, Bertrand P, Guigliarelli B
Title Nature and electronic structure of the Ni-X dinuclear center of Desulfovibrio gigas hydrogenase. Implications for the enzymatic mechanism.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9479448
Journal Biochimie
Year 1997
Volume 79
Pages 661-6
Authors Fontecilla-Camps JC, Frey M, Garcin E, Hatchikian C, Montet Y, Piras C, Vernede X, Volbeda A
Title Hydrogenase: a hydrogen-metabolizing enzyme. What do the crystal structures tell us about its mode of action?
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 9228943
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 523-6
Authors Montet Y, Amara P, Volbeda A, Vernede X, Hatchikian EC, Field MJ, Frey M, Fontecilla-Camps JC
Title Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 8990114
Journal Nature
Year 1997
Volume 385
Pages 126
Authors Happe RP, Roseboom W, Pierik AJ, Albracht SP, Bagley KA
Title Biological activation of hydrogen.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-552.
Medline ID
PubMed ID 9438867
Journal Structure
Year 1997
Volume 5
Pages 1671-80
Authors Higuchi Y, Yagi T, Yasuoka N
Title Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis.
Related PDB 1h2a
Related UniProtKB P21852 P21853
[21]
Resource
Comments
Medline ID
PubMed ID 9765886
Journal Biochem Soc Trans
Year 1998
Volume 26
Pages 396-401
Authors Garcin E, Montet Y, Volbeda A, Hatchikian C, Frey M, Fontecilla-Camps JC
Title Structural bases for the catalytic mechanism of [NiFe] hydrogenases.
Related PDB
Related UniProtKB
[22]
Resource
Comments X-ray Diffraction
Medline ID
PubMed ID 9751716
Journal Proc Natl Acad Sci U S A
Year 1998
Volume 95
Pages 11625-30
Authors Rousset M, Montet Y, Guigliarelli B, Forget N, Asso M, Bertrand P, Fontecilla-Camps JC, Hatchikian EC
Title [3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis.
Related PDB 1frf
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 10049702
Journal Biochem Biophys Res Commun
Year 1999
Volume 255
Pages 295-9
Authors Higuchi Y, Yagi T
Title Liberation of hydrogen sulfide during the catalytic action of Desulfovibrio hydrogenase under the atmosphere of hydrogen.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 9920874
Journal J Biol Chem
Year 1999
Volume 274
Pages 3331-7
Authors Pierik AJ, Roseboom W, Happe RP, Bagley KA, Albracht SP
Title Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe]-hydrogenases. NiFe(CN)2CO, Biology's way to activate H2.
Related PDB
Related UniProtKB
[25]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
Medline ID
PubMed ID 10378274
Journal Structure Fold Des
Year 1999
Volume 7
Pages 549-56
Authors Higuchi Y, Ogata H, Miki K, Yasuoka N, Yagi T
Title Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolution.
Related PDB 1h2r
Related UniProtKB P21852 P21853
[26]
Resource
Comments
Medline ID
PubMed ID 11128995
Journal J Biol Inorg Chem
Year 2000
Volume 5
Pages 682-91
Authors Bertrand P, Dole F, Asso M, Guigliarelli B
Title Is there a rate-limiting step in the catalytic cycle of Ni-Fe hydrogenases?
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 10766434
Journal J Biol Inorg Chem
Year 2000
Volume 5
Pages 36-44
Authors Trofanchuk O, Stein M, Gessner C, Lendzian F, Higuchi Y, Lubitz W
Title Single crystal EPR studies of the oxidized active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 11001090
Journal J Inorg Biochem
Year 2000
Volume 80
Pages 205-11
Authors Higuchi Y, Toujou F, Tsukamoto K, Yagi T
Title The presence of a SO molecule in [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki as detected by mass spectrometry.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 11170458
Journal Biochemistry
Year 2001
Volume 40
Pages 1317-24
Authors Fritz G, Griesshaber D, Seth O, Kroneck PM
Title Nonaheme cytochrome c, a new physiological electron acceptor for [Ni,Fe] hydrogenase in the sulfate-reducing bacterium Desulfovibrio desulfuricans Essex: primary sequence, molecular parameters, and redox properties..
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 11195380
Journal Inorg Chem
Year 2001
Volume 40
Pages 18-24
Authors Li S, Hall MB
Title Modeling the active sites of metalloenzymes. 4. Predictions of the unready states of [NiFe] Desulfovibrio gigas hydrogenase from density functional theory.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 11703120
Journal Inorg Chem
Year 2001
Volume 40
Pages 6201-3
Authors Niu S, Hall MB
Title Modeling the active sites in metalloenzymes 5. The heterolytic bond cleavage of H(2) in the [NiFe] hydrogenase of desulfovibrio gigas by a nucleophilic addition mechanism.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 11403633
Journal J Am Chem Soc
Year 2001
Volume 123
Pages 5839-40
Authors Stein M, van Lenthe E, Baerends EJ, Lubitz W
Title Relativistic DFT calculations of the paramagnetic intermediates of [NiFe] hydrogenase. Implications for the enzymatic mechanism.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 11372206
Journal J Biol Inorg Chem
Year 2001
Volume 6
Pages 467-73
Authors Fan HJ, Hall MB
Title Recent theoretical predictions of the active site for the observed forms in the catalytic cycle of Ni-Fe hydrogenase.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 11372204
Journal J Biol Inorg Chem
Year 2001
Volume 6
Pages 453-9
Authors Maroney MJ, Bryngelson PA
Title Spectroscopic and model studies of the Ni-Fe hydrogenase reaction mechanism.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 11191224
Journal J Biol Inorg Chem
Year 2001
Volume 6
Pages 63-81
Authors Matias PM, Soares CM, Saraiva LM, Coelho R, Morais J, Le Gall J, Carrondo MA
Title [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 A and modelling studies of its interaction with the tetrahaem cytochrome c3.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 11921392
Journal Chembiochem
Year 2002
Volume 3
Pages 153-60
Authors Frey M
Title Hydrogenases: hydrogen-activating enzymes.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 12184759
Journal Inorg Chem
Year 2002
Volume 41
Pages 4424-34
Authors Stadler C, de Lacey AL, Montet Y, Volbeda A, Fontecilla-Camps JC, Conesa JC, Fernandez VM
Title Density functional calculations for modeling the active site of nickel-iron hydrogenases. 2. Predictions for the unready and ready States and the corresponding activation processes.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 11782180
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 281-6
Authors Carepo M, Tierney DL, Brondino CD, Yang TC, Pamplona A, Telser J, Moura I, Moura JJ, Hoffman BM
Title 17O ENDOR detection of a solvent-derived Ni-(OH(x))-Fe bridge that is lost upon activation of the hydrogenase from Desulfovibrio gigas.
Related PDB
Related UniProtKB
[39]
Resource
Comments X-ray Diffraction
Medline ID
PubMed ID 12296727
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 11628-35
Authors Ogata H, Mizoguchi Y, Mizuno N, Miki K, Adachi S, Yasuoka N, Yagi T, Yamauchi O, Hirota S, Higuchi Y
Title Structural studies of the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F: suggestion for the initial activation site for dihydrogen.
Related PDB 1ubh 1ubj 1ubk 1ubl 1ubm 1ubo 1ubr 1ubt
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 11935356
Journal J Biol Inorg Chem
Year 2002
Volume 7
Pages 318-26
Authors De Lacey AL, Stadler C, Fernandez VM, Hatchikian EC, Fan HJ, Li S, Hall MB
Title IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 11862554
Journal J Biol Inorg Chem
Year 2002
Volume 7
Pages 177-94
Authors Muller A, Tscherny I, Kappl R, Hatchikian C, Huttermann J, Cammack R
Title Hydrogenases in the "active" state: determination of g-matrix axes and electron spin distribution at the active site by 1H ENDOR spectroscopy.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 12515509
Journal J Am Chem Soc
Year 2003
Volume 125
Pages
Authors Foerster S, Stein M, Brecht M, Ogata H, Higuchi Y, Lubitz W
Title Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 12459907
Journal J Biol Inorg Chem
Year 2003
Volume 8
Pages 129-34
Authors DeLacey AL, Fernandez VM, Rousset M, Cavazza C, Hatchikian EC
Title Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovoransNi-Fe hydrogenase.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 15062773
Journal Curr Opin Chem Biol
Year 2004
Volume 8
Pages 133-40
Authors Armstrong FA
Title Hydrogenases: active site puzzles and progress.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 14688251
Journal J Biol Chem
Year 2004
Volume 279
Pages 10508-13
Authors Dementin S, Burlat B, De Lacey AL, Pardo A, Adryanczyk-Perrier G, Guigliarelli B, Fernandez VM, Rousset M
Title A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 15365900
Journal J Biol Inorg Chem
Year 2004
Volume 9
Pages 873-84
Authors Bruschi M, De Gioia L, Zampella G, Reiher M, Fantucci P, Stein M
Title A theoretical study of spin states in Ni-S4 complexes and models of the [NiFe] hydrogenase active site.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 15175937
Journal J Biol Inorg Chem
Year 2004
Volume 9
Pages 636-42
Authors De Lacey AL, Pardo A, Fernandez VM, Dementin S, Adryanczyk-Perrier G, Hatchikian EC, Rousset M
Title FTIR spectroelectrochemical study of the activation and inactivation processes of [NiFe] hydrogenases: effects of solvent isotope replacement and site-directed mutagenesis.
Related PDB
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[48]
Resource
Comments
Medline ID
PubMed ID 15134933
Journal J Inorg Biochem
Year 2004
Volume 98
Pages 862-77
Authors Stein M, Lubitz W
Title Relativistic DFT calculation of the reaction cycle intermediates of [NiFe] hydrogenase: a contribution to understanding the enzymatic mechanism.
Related PDB
Related UniProtKB
[49]
Resource
Comments
Medline ID
PubMed ID 15667250
Journal Biochem Soc Trans
Year 2005
Volume 33
Pages 7-11
Authors van Gastel M, Fichtner C, Neese F, Lubitz W
Title EPR experiments to elucidate the structure of the ready and unready states of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F.
Related PDB
Related UniProtKB
[50]
Resource
Comments
Medline ID
PubMed ID 15803334
Journal J Biol Inorg Chem
Year 2005
Volume 10
Pages 239-49
Authors Volbeda A, Martin L, Cavazza C, Matho M, Faber BW, Roseboom W, Albracht SP, Garcin E, Rousset M, Fontecilla-Camps JC
Title Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.
Related PDB 1yq9 1yqw 1yrq
Related UniProtKB
[51]
Resource
Comments
Medline ID
PubMed ID 16271886
Journal Structure
Year 2005
Volume 13
Pages 1635-42
Authors Ogata H, Hirota S, Nakahara A, Komori H, Shibata N, Kato T, Kano K, Higuchi Y
Title Activation process of [NiFe] hydrogenase elucidated by high-resolution X-Ray analyses: conversion of the ready to the unready state.
Related PDB 1wuh 1wui 1wuj 1wuk 1wul
Related UniProtKB

Comments
This enzyme catalyzes the following reactions:
(A) Electron transfer from heme iron of cytochrome c3 to [4Fe-4S] cluster-2 located on the surface of small subunit:
(A1) His184 (1frf) bound to Fe4-S4, is exposed to the surface of the S subunit. This residue might interact with cytochrome c3, for electron transfer (see [12]).
(B) Electron transfer from [4Fe-4S] cluster-2 to [3Fe-4S] cluster:
(B1) Indirect transfer from [4Fe-4S] cluster-2 to [3Fe-4S] cluster through Cys218 (bound to [4Fe-4S] cluster-2) and Cys245 (bound to [3Fe-4S]) (see [12]).
(C) Electron transfer from [3Fe-4S] cluster to [4Fe-4S] cluster-1:
(C1) Indirect transfer from [3Fe-4S] cluster to [4Fe-4S] cluster-1 through Cys248 (bound to [3Fe-4S]) and Cys147 (bound to [4Fe-4S] cluster-1) (see [12]).
(D) Electron transfer from [4Fe-4S] cluster-1 to the Nickel-Iron cluster (reaction center):
(D1) Indirect transfer from [4Fe-4S] cluster-1 to Nickel-Iron cluster through Cys17 (bound to [4Fe-4S] cluster-1) and Cys72 of Large subunit (bound to Nickel-Iron cluster) (see [12]).
(E) Hydrogenation at the Nickel-Iron cluster (reaction center):

Created Updated
2005-08-12 2009-02-26