Proceedings of the National Academy of Sciences · 1978 · 279 citations · 16 references
Life SciencesBiochemistryBiologyEnzyme MechanismEnzymologyRedox BiochemistryAtp HydrolysisCatalytic MechanismsElectron Transfer In ProteinsEnzyme KineticsRedox EnzymesAtp Hydrolysis MechanismCatalytic Cycle DynamicsElectron TransferElectron Transfer In EnzymesHydrogen EvolutionHydrogen Evolution KineticsHydrogen Evolution ReactionLag Phase
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.
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The estimation of creatine and of diacetyl
Philip Eggleton, S. R. Elsden, Nancy R. Gough · Biochemical Journal · 1943 · 256 citations · Full text
William H. Orme‐Johnson, William Hamilton, T. L. Jones et al. · Proceedings of the National Academy of Sciences · 1972 · 169 citations · Full text