Biological activity and nitrogen fixation

Finally, in 1797, the Frenchman L. N. Vauquelin discovered the oxide of a new element in a Siberian mineral, now known as crocoite (PbCr04), and in the following year isolated the metal itself by charcoal reduction. This was subsequently named chromium (Greek xpco ia, chroma, colour) because of the variety of colours found in its compounds. Since their discoveries the metals and their compounds have become vitally important in many industries and, as one of the biologically active transition elements, molybdenum has been the subject of a great deal of attention in recent years, especially in the field of nitrogen fixation (p. 1035). 

At the same time, this redox lability makes Mo well suited as a cofactor in enzymes that catalyze redox reactions. An example is the prominence of Mo in nitrogen fixation. This prokaryotic metabolism, the dominant pathway for conversion of atmospheric Nj to biologically-useful NH, utilizes Mo (along with Fe) in the active site of the nitrogenase enzyme that catalyzes Nj reduction. Alternative nitrogenases that do not incorporate Mo have been identified, but are markedly less efficient (Miller and Eady 1988 Eady 1996). 

The electrosynthesis of hydride complexes directly from molecular hydrogen at atmospheric pressure by reduction of Mo(II) and W(II) tertiary phosphine precursors in moderate yield has been described as also the electrosynthesis of trihydride complexes of these metals by reduction of M(IV) dihydride precursors [101,102]. Hydrogen evolution at the active site of molybdenum nitrogenases [103] is intimately linked with biological nitrogen fixation and the electrochemistry of certain well-defined mononuclear molybdenum and tungsten hydrido species has been discussed in this context [104,105]. 

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