KEGG ENZYME: 1.12.2.1

ENZYME: 1.12.2.1

Entry

EC 1.12.2.1                 Enzyme

Name

cytochrome-c3 hydrogenase;
H2:ferricytochrome c3 oxidoreductase;
cytochrome c3 reductase;
cytochrome hydrogenase;
hydrogenase [ambiguous]

Class

Oxidoreductases;
Acting on hydrogen as donor;
With a cytochrome as acceptor

Sysname

hydrogen:ferricytochrome-c3 oxidoreductase

Reaction(IUBMB)

H2 + 2 ferricytochrome c3 = 2 H+ + 2 ferrocytochrome c3 [RN:R04015]

Reaction(KEGG)

R04015

Substrate

H2 [CPD:C00282];
ferricytochrome c3 [CPD:C02682]

Product

H+ [CPD:C00080];
ferrocytochrome c3 [CPD:C02684]

Comment

An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.

History

EC 1.12.2.1 created 1972, modified 2002

Orthology

K00437

[NiFe] hydrogenase large subunit

K18008

[NiFe] hydrogenase small subunit

Genes

MELL:

IVG45_04075

HTM:	RZR91_08890

NAM:

NAMH_1007

NAP:	C3L23_02965

HMR:	Hipma_1098

GSB:	GSUB_14145

GHC:	L9S41_08545 L9S41_13340

DEU:

DBW_3352

DVE:	DESUT3_36440

DES:	DSOUD_3281(hybL)

DDS:	Ddes_1038 Ddes_1039

DFI:	AXF13_05345 AXF13_05350

DPG:	DESPIGER_2408 DESPIGER_2409

DEF:	CNY67_06350 CNY67_06355

DTR:	RSDT_0750(hynA) RSDT_0751(hynB)

DFL:	DFE_1090 DFE_1091

PSYF:

N1030_05840 N1030_05845

DSB:	LN040_03705 LN040_03710 LN040_10885 LN040_10890

DMA:	DMR_15600 DMR_15610

DCB:	C3Y92_13765 C3Y92_13770

DGG:	DGI_2261(hydB) DGI_2262(hydA)

DDE:	Dde_2137 Dde_2138 Dde_3755 Dde_3756

DMS:	E8L03_04605 E8L03_04610

DSA:	Desal_1915 Desal_1916

DHY:	DESAM_22353(hybC) DESAM_22354(hydA)

DAF:	Desaf_3127 Desaf_3128

DAS:	Daes_2582 Daes_2583

DPI:	BN4_11411(hynB-1) BN4_11412(hynA-1) BN4_12036(hynA) BN4_12037(hynB)

DEJ:	AWY79_10910 AWY79_10915 AWY79_15475 AWY79_15480

PPRF:

DPRO_2872(hydA) DPRO_2873(hybC) DPRO_3463(hydB) DPRO_3464(hynB)

PSEL:

GM415_00940 GM415_00945

DDN:	DND132_3240 DND132_3241

PSEF:

PSDVSF_33320(hynB1) PSDVSF_33330(hynA-1)

PPOR:

JCM14722_26830(hynB1) JCM14722_26840(hynA-1)

PNW:	SYK_14410(hynA-1_1) SYK_32520(hynB1) SYK_32530(hynA-1_2)

PTHE:

LF599_05010 LF599_05015

PMEN:

V8V93_01455 V8V93_08215 V8V93_08220

DSX:	GD604_03825 GD604_03830 GD604_12480

DSD:	GD606_11990 GD606_18650 GD606_18655

PBIZ:

LWC08_05010 LWC08_05015

DVU:	DVU_1921(hynB-1) DVU_1922(hynA-1) DVU_2525(hynB-2) DVU_2526(hynA-2)

DVL:	Dvul_0718 Dvul_0719 Dvul_1245 Dvul_1246

DVM:	DvMF_0270 DvMF_0271 DvMF_1732 DvMF_1733

DVG:	Deval_1388 Deval_1389 Deval_2330 Deval_2331

CLIH:

KPS_000369 KPS_000370 KPS_001976 KPS_001977

TMUR:

JBF11_08395 JBF11_08400

DBA:	Dbac_0766 Dbac_0767

DESU:

NLA06_03975 NLA06_03980

THEW:

TDMWS_05530(hynB1) TDMWS_05540(hynA-1)

DRT:	Dret_0265(hydB) Dret_0266(hydA)

DPS:

DP0159

DSF:

UWK_01156

DAK:	DaAHT2_0520 DaAHT2_0675

DAL:	Dalk_2275 Dalk_2276

DAT:	HRM2_22350(hynB) HRM2_22360(hynA)

DTO:	TOL2_C39190(hysB)

DHG:	EYB58_03620 EYB58_03625

DWD:	DSCW_35860(hynA-1) DSCW_35870(hynB1)

DALK:

DSCA_34960(hynA-1) DSCA_34970(hynB1_1) DSCA_49780 DSCA_49790(hynB1_2)

DVR:	Dvar_81470 Dvar_81480

DLI:	dnl_48300(hynA) dnl_48320(hynB)

DTI:	Desti_3745 Desti_3746

SFU:	Sfum_2952 Sfum_2953

DAX:	FDQ92_06195 FDQ92_06200

DBR:	Deba_0998 Deba_1400 Deba_1401

DMP:	FAK_26530(hynA-1) FAK_26540

TOP:	TOPB45_0886

TNR:	Thena_0337

TACI:

TDSAC_0333

DIN:	Selin_0442

OCW:	OW730_19290

SLP:

Slip_0386

DSY:

DSY1598

DHD:

Dhaf_2742

DDH:	Desde_2202

DDL:	Desdi_1872

DOR:	Desor_0911

DAI:	Desaci_3499

DMI:	Desmer_0911

DED:	DHBDCA_p1839

DEC:	DCF50_p1850

DRS:	DEHRE_02790

PTH:	PTH_1702(HyaB)

AACX:

DEACI_0833

TJR:	TherJR_0258 TherJR_0765

CTHM:

CFE_1479

DAU:

Daud_1042

CHY:

CHY_1545

ADG:

Adeg_1231

TPZ:	Tph_c06360

CALK:

HUE98_09375

CCU:	Ccur_08540

SHI:	Shel_12910

ELE:

Elen_1276

EYY:	EGYY_12340(HyaB)

EGD:	GS424_006745

GPA:

GPA_23430

AEQ:

AEQU_1238

AHAT:

ADCFC_11360(hynA-1)

DDT:	AAY81_05105

CBAC:

JI75_02035

BWA:	HLV38_03365

RTS:	CE91St31_14000(hynA-1)

EBZ:	J7S26_02745

DET:

DET0110

DEH:	cbdbA129(hupL)

DEB:	DehaBAV1_0258

DEV:	DhcVS_120(hupL)

DEG:	DehalGT_0141

DMC:	btf_72(hupL)

DMD:	dcmb_135(hupL)

DMG:	GY50_0142(hupL)

DMX:	X792_00720

DMY:	X793_00585

DMZ:	X794_00505

DUC:	UCH007_00970(hupL)

DLY:	Dehly_0025 Dehly_1288

DEW:	DGWBC_0126 DGWBC_0300

DFO:	Dform_01919(hyaB\|hybC) Dform_01922(hyaB\|hybC)

DETH:

HX448_00350 HX448_00425

DLF:	V8247_02405 V8247_04695

» show all

Reference

1 [PMID:4364940]

Authors

Der Vartanian DV, LeGall J.

Title

A monomolecular electron transfer chain: structure and function of cytochrome C3.

Journal

Biochim Biophys Acta 346:79-99 (1974)
DOI:10.1016/0304-4173(74)90012-3

Reference

2 [PMID:3546297]

Authors

Higuchi Y, Yasuoka N, Kakudo M, Katsube Y, Yagi T, Inokuchi H.

Title

Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F.

Journal

J Biol Chem 262:2823-5 (1987)

Sequence

[dvm:DvMF_0270 DvMF_0271]

Reference

3 [PMID:13741672]

Authors

RIKLIS E, RITTENBERG D.

Title

Some observations on the enzyme, hydrogenase.

Journal

J Biol Chem 236:2526-9 (1961)

Reference

4 [PMID:13745271]

Authors

SADANA JC, MOREY AV.

Title

Purification and properties of the hydrogenase of Desulfovibrio desulfuricans.

Journal

Biochim Biophys Acta 50:153-63 (1961)
DOI:10.1016/0006-3002(61)91072-1

Reference

5 [PMID:7854413]

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.

Journal

Nature 373:580-7 (1995)
DOI:10.1038/373580a0

Sequence

[dgg:DGI_2261 DGI_2262]

Reference

6 [PMID:10378275]

Authors

Garcin E, Vernede X, Hatchikian EC, Volbeda A, Frey M, Fontecilla-Camps JC.

Title

The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center.

Journal

Structure 7:557-66 (1999)
DOI:10.1016/S0969-2126(99)80072-0

Sequence

[dgg:DGI_2261 DGI_2262]

Other DBs

ExplorEnz - The Enzyme Database:

1.12.2.1

IUBMB Enzyme Nomenclature:

1.12.2.1

ExPASy - ENZYME nomenclature database:

1.12.2.1

UM-BBD (Biocatalysis/Biodegradation Database):

1.12.2.1

BRENDA, the Enzyme Database:

1.12.2.1

CAS:

9027-05-8

DBGET integrated database retrieval system