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Nonenzymatic Simulation of Nitrogenase Reactions and the Mechanism of Biological Nitrogen Fixation
Author(s) -
Schrauzer G. N.
Publication year - 1975
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.197505141
Subject(s) - nitrogenase , chemistry , molybdenum , nitrogen fixation , nitrogen , active site , redox , inorganic chemistry , enzyme , biochemistry , organic chemistry
The development of biologically relevant model systems of nitrogenase permitted the simulation of virtually all known reactions of the nitrogen reducing enzymes under nonenzymatic conditions. On the basis of these experiments, a mechanism of biological nitrogen fixation is formulated which is in accord with the available enzymological evidence. The key reactions of the substrates of nitrogenase occur at a molybdenum active site. The non‐heme iron, which is bound to sulfur and protein‐S ⊝ groups, mediates the transport of electrons to the molybdenum active site but does not participate directly in the reduction of the substrates. ATP is required for the acceleration of the reduction and activation of the molybdenum site and is hydrolyzed to ADP and inorganic phosphate. Diimine and hydrazine were detected as intermediates in the reduction of molecular nitrogen under nonenzymatic conditions.