Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle

Proc Natl Acad Sci U S A. 1978 Jun;75(6):2699-702. doi: 10.1073/pnas.75.6.2699.

Abstract

Nitrogenase and nitrogenase reductase dissociate after each electron is transferred between them, as shown by the occurrence of a lag phase approximately as long as the average turnover time of nitrogenase before hydrogen evolution occurs. Because nitrogenase was present in the reaction mixture in large excess over nitrogenase reductase, the electrons donated by nitrogenase reductase must have been distributed randomly over all of the nitrogenase present. This is accomplished by nitrogenase reductase molecules associating randomly with nitrogenase molecules for each cycle of electrons transferred. The fact that ATP is hydrolyzed without a lag indicates both that electron transfer occurs during the lag and the ATP hydrolysis is coupled to electron transfer from nitrogenase reductase to nitrogenase and not to substrate reduction. The observations support the suggestion that it now is desirable to alter nomenclature to designate the MoFe protein as nitrogenase and the Fe protein as nitrogenase reductase.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Catalysis
  • Electron Transport
  • Flavodoxin / metabolism
  • Hydrogen / metabolism
  • Kinetics
  • Macromolecular Substances
  • Multienzyme Complexes / metabolism*
  • Nitrogenase / metabolism*

Substances

  • Flavodoxin
  • Macromolecular Substances
  • Multienzyme Complexes
  • Hydrogen
  • Adenosine Triphosphate
  • Nitrogenase