Abstract
Sulfur donors are prominent even in crude chemical descriptions of nitrogenase and are likely to be of importance in other molybdoenzymes. Recently, extended X-ray absorption fine structure studies have confirmed that molybdenum is indeed coordinated to sulfur in the Mo-Fe protein derived from Clostridium pasteurianum.1 A study of the fundamental chemistry of Mo-S donor complexes is a logical accompaniment to understanding the more complex enzyme systems. For this reason, we are investigating molybdenum complexes in which the predominant donor is sulfur and where the coligands are those having significance in nitrogen fixation research. For example, one suggested pathway for reduction of N2 to ammonia involves N2 bridging between two molybdenum atoms to produce, in turn, bridged diazene and hydrazine complex intermediates and finally, a labile ammonia complex.2
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