CATH Classification

Domain Context

CATH Clusters

Superfamily Nitrogenase molybdenum iron protein domain
Functional Family

Enzyme Information

1.18.6.1
Nitrogenase.
based on mapping to UniProt P07328
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.
-!- The enzyme is a complex of two components (namely dinitrogen reducatse and dinitrogenase). -!- Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of two molecules of ATP, transfers an electron from ferredoxin to the dinitrogenase component. -!- Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazene and hydrazine. -!- 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). -!- The enzyme does not reduce CO (cf. EC 1.18.6.2). -!- Formerly EC 1.18.2.1.

UniProtKB Entries (1)

P00459
NIFH1_AZOVI
Azotobacter vinelandii
Nitrogenase iron protein 1

PDB Structure

PDB 4WZA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural evidence for asymmetrical nucleotide interactions in nitrogenase.
Tezcan, F.A., Kaiser, J.T., Howard, J.B., Rees, D.C.
J.Am.Chem.Soc.