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IUBMB CommentsRequires 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].
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12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O
12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate
acetylene + H2 + ?
ethylene + ?
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CO + ATP + dithionite + ?
ethene + ethane + propane + ?
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CO + H+ + ATP
C2H4 + C2H6 + C3H8 + H2O + H2 + phosphate
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12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O
12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate
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12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O
12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate
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12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O
12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate
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12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O
12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate
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additional information
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enzym also forms ethane continuously at a rate of 2.1% of that of ethylene
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enzym also forms ethane continuously at a rate of 2.1% of that of ethylene
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additional information
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enzym also forms ethane continuously at a rate of 2.1% of that of ethylene
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additional information
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enzym also forms ethane continuously at a rate of 2.1% of that of ethylene
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additional information
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the efficiency of ATP hydrolysis coupled to substrate reduction (ATP/2e ratio) is 4.87 at 30°C during the reduction of protons to H2 and 7.16 during the reduction of N2
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additional information
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the efficiency of ATP hydrolysis coupled to substrate reduction (ATP/2e ratio) is 4.87 at 30°C during the reduction of protons to H2 and 7.16 during the reduction of N2
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physiological function
a deletion in the VnfD, VnfG and VnfK gene cluster prevents V-dependent nitrogen fixation. A strain defective in both V-nitrogenase and Mo-nitrogenase (EC 1.18.6.1) structural genes shows no residual nitrogen fixing capacity
physiological function
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a nifB mutant lacking a small Fe-S cluster that is a precursor of FeMo-co, is unable to grow diazotrophically, even in presence of vanadium, in the absence of molybdenum
physiological function
an insertion mutant in VnfY has 10fold less V-containing nitrogenase activity and exhibits a greatly diminished level of V label incorporation into the V-dependent dinitrogenase when compared to the wild-type. VnfY is involved in the biosynthesis or insertion of FeV-co into the V-containing dinitrogenase
physiological function
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a deletion in the VnfD, VnfG and VnfK gene cluster prevents V-dependent nitrogen fixation. A strain defective in both V-nitrogenase and Mo-nitrogenase (EC 1.18.6.1) structural genes shows no residual nitrogen fixing capacity
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physiological function
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an insertion mutant in VnfY has 10fold less V-containing nitrogenase activity and exhibits a greatly diminished level of V label incorporation into the V-dependent dinitrogenase when compared to the wild-type. VnfY is involved in the biosynthesis or insertion of FeV-co into the V-containing dinitrogenase
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Dilworth, M.; Eldridge, M.; Eady, R.
Correction for creatine interference with the direct indophenol measurement of NH3 in steady-state nitrogenase assays
Anal. Biochem.
207
6-10
1992
Azotobacter chroococcum (P15332 and P15334 and P15333), Azotobacter chroococcum MCD1 (P15332 and P15334 and P15333)
brenda
Lee, C.; Hu, Y.; Ribbe, M.
Tracing the hydrogen source of hydrocarbons formed by vanadium nitrogenase
Angew. Chem. Int. Ed. Engl.
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2011
Azotobacter vinelandii
brenda
Boison, G.; Steingen, C.; Stal, L.J.; Bothe, H.
The rice field cyanobacteria Anabaena azotica and Anabaena sp. CH1 express vanadium-dependent nitrogenase
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2006
Anabaena azotica (Q6TFK2), Anabaena azotica, Anabaena azotica FACHB-118 (Q6TFK2), Anabaena azotica FACHB-118
brenda
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The vanadium nitrogenase of Azotobacter chroococcum. Purification and properties of the VFe protein
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Azotobacter chroococcum (P15332 and P15334 and P15333), Azotobacter chroococcum MCD1 (P15332 and P15334 and P15333)
brenda
Eady, R.; Richardson, T.; Miller, R.; Hawkins, M.; Lowe, D.
The vanadium nitrogenase of Azotobacter chroococcum. Purification and properties of the Fe protein
Biochem. J.
256
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1988
Azotobacter chroococcum (P15332 and P15334 and P15333), Azotobacter chroococcum MCD1 (P15332 and P15334 and P15333)
brenda
Miller, R.; Eady, R.
Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature favours N2 reduction by vanadium nitrogenase
Biochem. J.
256
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1988
Azotobacter chroococcum
brenda
Thorneley, R.; Bergström, N.; Eady, R.; Lowe, D.
Vanadium nitrogenase of Azotobacter chroococcum. MgATP-dependent electron transfer within the protein complex
Biochem. J.
257
789-794
1989
Azotobacter chroococcum (P15332 and P15334 and P15333), Azotobacter chroococcum MCD1 (P15332 and P15334 and P15333)
brenda
Dilworth, M.; Eldridge, M.; Eady, R.
The molybdenum and vanadium nltrogenases of Azotobacter chroococcum Effect of elevated temperature on N2 reduction
Biochem. J.
289
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1993
Azotobacter chroococcum (P15332 and P15334 and P15333), Azotobacter chroococcum MCD1 (P15332 and P15334 and P15333)
brenda
Robson, R.; Woodley, P.; Pau, R.; Eady, R.
Structural genes for the vanadium nitrogenase from Azotobacter chroococcum
EMBO J.
8
1217-1224
1989
Azotobacter chroococcum (P15332 and P15334 and P15333), Azotobacter chroococcum MCD1 (P15332 and P15334 and P15333)
brenda
Lyons, E.M.; Thiel, T.
Characterization of nifB, nifS, and nifU genes in the cyanobacterium Anabaena variabilis NifB is required for the vanadium-dependent nitrogenase
J. Bacteriol.
177
1570-1575
1995
Trichormus variabilis
brenda
Ruettimann-Johnson, C.; Rubio, L.; Dean, D.; Ludden, P.
VnfY is required for full activity of the vanadium-containing dinitrogenase in Azotobacter vinelandii
J. Bacteriol.
185
2383-2386
2003
Azotobacter vinelandii (C1DI21), Azotobacter vinelandii DJ (C1DI21)
brenda
Sippel, D.; Schlesier, J.; Rohde, M.; Trncik, C.; Decamps, L.; Djurdjevic, I.; Spatzal, T.; Andrade, S.L.; Einsle, O.
Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion
J. Biol. Inorg. Chem.
22
161-168
2017
Azotobacter vinelandii
brenda
Sippel, D.; Einsle, O.
The structure of vanadium nitrogenase reveals an unusual bridging ligand
Nat. Chem. Biol.
13
956-960
2017
Azotobacter vinelandii (P16855)
brenda
Lee, C.; Hu, Y.; Ribbe, M.
Vanadium nitrogenase reduces CO
Science
329
642
2010
Azotobacter vinelandii
brenda