CATH Classification

Domain Context

CATH Clusters

Superfamily Nitrogenase molybdenum iron protein domain
Functional Family Nitrogenase protein alpha chain

Enzyme Information
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.
-!- 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 -!- Formerly EC

UniProtKB Entries (1)

Azotobacter vinelandii
Nitrogenase molybdenum-iron protein beta chain

PDB Structure

External Links
Primary Citation
Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase.
Spatzal, T., Perez, K.A., Einsle, O., Howard, J.B., Rees, D.C.