KEGG   ENZYME: 1.18.6.2
Entry
EC 1.18.6.2                 Enzyme                                 
Name
vanadium-dependent nitrogenase;
vnfD (gene name);
vnfG (gene name);
vnfK (gene name)
Class
Oxidoreductases;
Acting on iron-sulfur proteins as donors;
With dinitrogen as acceptor
Sysname
ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing, vanadium-dependent)
Reaction(IUBMB)
12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O = 12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate [RN:R12084]
Reaction(KEGG)
R12084
Substrate
reduced ferredoxin [CPD:C00138];
H+ [CPD:C00080];
N2 [CPD:C00697];
ATP [CPD:C00002];
H2O [CPD:C00001]
Product
oxidized ferredoxin [CPD:C00139];
H2 [CPD:C00282];
NH3 [CPD:C00014];
ADP [CPD:C00008];
phosphate [CPD:C00009]
Comment
Requires Mg2+. This enzyme, originally isolated from the bacterium Azotobacter vinelandii, is a complex of two components (namely dinitrogen reductase and dinitrogenase). Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of ATP, transfers an electron from ferredoxin to the dinitrogenase component. Dinitrogenase is a vanadium-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazine and hydrazine. Compared with molybdenum-dependent nitrogenase (EC 1.18.6.1), this enzyme produces more dihydrogen and consumes more ATP per dinitrogen molecule being reduced. Unlike EC 1.18.6.1, this enzyme can also use CO as substrate, producing ethene, ethane and propane [7,9].
History
EC 1.18.6.2 created 2018
Pathway
ec00910  Nitrogen metabolism
ec01100  Metabolic pathways
ec01310  Nitrogen cycle
Orthology
K22896  vanadium-dependent nitrogenase alpha chain
K22897  vanadium-dependent nitrogenase beta chain
K22898  vanadium nitrogenase delta subunit
Genes
AVN: Avin_02590(vnfK) Avin_02600(vnfG) Avin_02610(vnfD)
AVL: AvCA_02590(vnfK) AvCA_02600(vnfG) AvCA_02610(vnfD)
AVD: AvCA6_02590(vnfK) AvCA6_02600(vnfG) AvCA6_02610(vnfD)
ACX: Achr_2510(vnfK) Achr_2520(vnfG) Achr_2530(vnfD)
MMOB: F6R98_01750(vnfK) F6R98_01755(vnfG) F6R98_01760(vnfD)
AIQ: Azoinq_00320(vnfK) Azoinq_00325(vnfG) Azoinq_00330(vnfD)
RPA: TX73_007075(vnfD) TX73_007080(vnfG) TX73_007085(vnfK)
RVA: Rvan_0514 Rvan_0515 Rvan_0516
MBRY: B1812_06630 B1812_06635 B1812_06640
MHEY: H2LOC_000350 H2LOC_000355(vnfG) H2LOC_000360(vnfD)
MPAR: F7D14_08705(vnfD) F7D14_08710(vnfG) F7D14_08715
RAP: RHOA_0303(vnfD) RHOA_0304(vnfG) RHOA_0305(vnfK)
ABS: AZOBR_p350020(nifD) AZOBR_p350021(vnfG) AZOBR_p350022(nifK)
DVN: HQ394_14350 HQ394_14360(vnfD)
DEK: DSLASN_18020
PDU: PDUR_11790 PDUR_11795 PDUR_11800
CKL: CKL_1745(vnfK) CKL_1746(vnfG) CKL_1747(vnfD)
CKR: CKR_1618 CKR_1619 CKR_1620
CPAS: Clopa_3471 Clopa_3472 Clopa_3473
CPAT: CLPA_c14260(vnfD) CLPA_c14270 CLPA_c14280(vnfK)
CPAE: CPAST_c14260(vnfD) CPAST_c14270 CPAST_c14280(vnfK)
EHA: Ethha_2312 Ethha_2313 Ethha_2314
MANA: MAMMFC1_00447(anfK_2) MAMMFC1_00448(vnfG) MAMMFC1_00449(vnfD_2)
NCW: NIES2107_08220 NIES2107_08230 NIES2107_08530
NOSQ: PQG02_36490(vnfD) PQG02_36980 PQG02_36990(vnfD)
AVA: Ava_4026 Ava_4027
ANN: EH233_18385(vnfK) EH233_18390(vnfD)
MDP: NIES3275_32040
TTQ: NIES37_39140 NIES37_39150 NIES37_39370
ALAX: NIES50_47220 NIES50_47440 NIES50_47450
MBA: Mbar_A2276 Mbar_A2277 Mbar_A2278
MBY: MSBRM_1347 MSBRM_1348 MSBRM_1349
MBW: MSBRW_2468 MSBRW_2469 MSBRW_2470
MBAR: MSBR2_1060 MSBR2_1061 MSBR2_1062
MBAK: MSBR3_1011 MSBR3_1012 MSBR3_1013
MAC: MA_1216(vnfD) MA_1217(vnfG) MA_1218(vnfK)
MVC: MSVAZ_2227 MSVAZ_2228 MSVAZ_2229
MEK: MSKOL_2226 MSKOL_2227 MSKOL_2228
MSJ: MSSAC_3362 MSSAC_3363 MSSAC_3364
MSZ: MSSIH_2887 MSSIH_2888 MSSIH_2889
MSW: MSSIT_2931 MSSIT_2932 MSSIT_2933
 » show all
Reference
1  [PMID:2851977]
  Authors
Eady RR, Richardson TH, Miller RW, Hawkins M, Lowe DJ
  Title
The vanadium nitrogenase of Azotobacter chroococcum. Purification and properties  of the Fe protein.
  Journal
Biochem J 256:189-96 (1988)
DOI:10.1042/bj2560189
Reference
2  [PMID:3223922]
  Authors
Miller RW, Eady RR
  Title
Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature  favours N2 reduction by vanadium nitrogenase.
  Journal
Biochem J 256:429-32 (1988)
DOI:10.1042/bj2560429
Reference
3  [PMID:2784670]
  Authors
Thorneley RN, Bergstrom NH, Eady RR, Lowe DJ
  Title
Vanadium nitrogenase of Azotobacter chroococcum. MgATP-dependent electron transfer within the protein complex.
  Journal
Biochem J 257:789-94 (1989)
DOI:10.1042/bj2570789
Reference
4  [PMID:1336937]
  Authors
Dilworth MJ, Eldridge ME, Eady RR
  Title
Correction for creatine interference with the direct indophenol measurement of NH3 in steady-state nitrogenase assays.
  Journal
Anal Biochem 207:6-10 (1992)
DOI:10.1016/0003-2697(92)90491-O
Reference
5  [PMID:8424785]
  Authors
Dilworth MJ, Eldridge ME, Eady RR
  Title
The molybdenum and vanadium nitrogenases of Azotobacter chroococcum: effect of elevated temperature on N2 reduction.
  Journal
Biochem J 289 ( Pt 2):395-400 (1993)
DOI:10.1042/bj2890395
Reference
6
  Authors
Eady RR.
  Title
Current status of structure function relationships of vanadium nitrogenase.
  Journal
Coordinat Chem Rev 237:23-30 (2003)
Reference
7  [PMID:20689010]
  Authors
Lee CC, Hu Y, Ribbe MW
  Title
Vanadium nitrogenase reduces CO.
  Journal
Science 329:642 (2010)
DOI:10.1126/science.1191455
Reference
8  [PMID:21538750]
  Authors
Lee CC, Hu Y, Ribbe MW
  Title
Tracing the hydrogen source of hydrocarbons formed by vanadium nitrogenase.
  Journal
Angew Chem Int Ed Engl 50:5545-7 (2011)
DOI:10.1002/anie.201100869
Reference
9  [PMID:28692069]
  Authors
Sippel D, Einsle O
  Title
The structure of vanadium nitrogenase reveals an unusual bridging ligand.
  Journal
Nat Chem Biol 13:956-960 (2017)
DOI:10.1038/nchembio.2428
Other DBs
ExplorEnz - The Enzyme Database: 1.18.6.2
IUBMB Enzyme Nomenclature: 1.18.6.2
ExPASy - ENZYME nomenclature database: 1.18.6.2
BRENDA, the Enzyme Database: 1.18.6.2

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