1.19.6.1: nitrogenase (flavodoxin)

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For detailed information about nitrogenase (flavodoxin), go to the full flat file.

Word Map on EC 1.19.6.1

1.19.6.1

azotobacter

vinelandii

mgadp

mofe-protein

molybdenum-iron

nifu

rhodospirillum

dinitrogenase

femo-cofactor

pasteurianum

mgadp-bound

bacteriochlorophyll

nucleotide-bound

nitrogenases

dark-operative

nucleotide-induced

protochlorophyllide

agriculture

Reaction

4 reduced flavodoxin + 2 H+ +

+ 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ +

+ 16 ADP + 16 phosphate

Synonyms

FeP, FldA, NifF, nitrogenase, nitrogenase Fe protein, nitrogenase Fe-protein

ECTree

1 Oxidoreductases

1.19 Acting on reduced flavodoxin as donor

1.19.6 With dinitrogen as acceptor

1.19.6.1 nitrogenase (flavodoxin)

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Results	in table
1	AA Sequence
1	Application
1	CAS Registry Number
2	Cloned(Commentary)
12	Cofactor
1	Crystallization (Commentary)
6	Inhibitors
1	KM Value [mM]
14	Metals/Ions
1	Molecular Weight [Da]
17	Natural Substrates/ Products (Substrates)
33	Organism
1	Oxidation Stability
6	Pathway
2	pH Optimum
13	Protein Variants
2	Purification (Commentary)
6	Reaction
3	Reaction Type
21	Reference
1	Source Tissue
3	Specific Activity [micromol/min/mg]
53	Substrates and Products (Substrate)
6	Subunits
7	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 1.19.6.1 - nitrogenase (flavodoxin)

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reduced flavodoxin:dinitrogen oxidoreductase (ATP-hydrolysing)

Requires Mg2+. It is composed of two components, dinitrogen reductase and dinitrogenase, that can be separated but are both required for nitrogenase activity. Dinitrogen reductase is a [4Fe-4S] protein, which, at the expense of ATP, transfers electrons from a dedicated flavodoxin to dinitrogenase. Dinitrogenase is a protein complex that contains either a molybdenum-iron cofactor, a vanadium-iron cofactor, or an iron-iron cofactor, that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia. The reduction is initiated by formation of hydrogen. The enzyme can also reduce acetylene to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Some enzymes utilize ferredoxin rather than flavodoxin as the electron donor (see EC 1.18.6.1, nitrogenase).