KEGG   ENZYME: 1.18.6.2Help
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
BRITE hierarchy
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)
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-depedent 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
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)
RPA: RPA1378(vnfD) RPA1379(vnfG) RPA1380(vnfK)
RVA: Rvan_0514 Rvan_0515 Rvan_0516
MBRY: B1812_06630 B1812_06635 B1812_06640
ABS: AZOBR_p350020(nifD) AZOBR_p350021(vnfG) AZOBR_p350022(nifK)
PDU: PDUR_11790 PDUR_11795 PDUR_11800
CKL: CKL_1745(vnfK) CKL_1746(vnfG) CKL_1747(vnfD)
MAC: MA_1216(vnfD) MA_1217(vnfG) MA_1218(vnfK)
 » show all
Taxonomy
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)
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)
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)
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)
Reference
6
  Authors
Eady, R.R.
  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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