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CATH Classification

Domain Context

CATH Clusters

Superfamily P-loop containing nucleotide triphosphate hydrolases
Functional Family Nitrogenase iron protein 4

Enzyme Information

1.18.6.1
Nitrogenase.
based on mapping to UniProt P00456
8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 phosphate.
-!- Composed of two proteins that can be separated but are both required for nitrogenase activity. -!- Dinitrogen reductase is a [4Fe-4S] protein, which, with two molecules of ATP and ferredoxin, generates an electron. -!- The electron is transferred to the other protein, dinitrogenase (molybdoferredoxin). -!- Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia; the molybdenum may be replaced by vanadium or iron. -!- The reduction is initiated by formation of hydrogen in stoichiometric amounts. -!- Acetylene is reduced 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. -!- Ferredoxin may be replaced by flavodoxin (see EC 1.19.6.1). -!- Formerly EC 1.18.2.1.

UniProtKB Entries (1)

P00456
NIFH1_CLOPA
Clostridium pasteurianum
Nitrogenase iron protein 1

PDB Structure

PDB 1CP2
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum.
Schlessman, J.L., Woo, D., Joshua-Tor, L., Howard, J.B., Rees, D.C.
J.Mol.Biol.
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