Nitrogenase electrochemistry

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]. 

Kala-Azar, 278 Keggin anions, 1034 electrochemistry, 1050 Keggin structures, 1035 heteropolyanions, 1037 Klebsiella pneumoniae nitrogenases, 1425 Kroll process, 325 Krypton compounds difluorides, 313 fluoride, 313... 

These enzymes continue to be the subject of intense research efforts, and this is a direct result of their unusual geometric and electronic structures, their key roles in the global C, N and S cycles, their pharmacological importance, and their importance in human health. This volume will detail how spectroscopy, structure, electrochemistry and theory have been used to develop a comprehensive description of the active site electronic structure contributions to reactivity in pyranopterin Mo enzymes and the Mo-dependent nitrogenase. A particular emphasis is placed on how these important studies have been used to reveal critical components of enzyme mechanisms. 

ELECTROCHEMISTRY OF THE IRON-MOLYBDENUM COFACTOR OF NITROGENASE EVIDENCE FOR MULTIPLE SPECIATION AND ELECTROCATALYTIC BEHAVIOR... 

Electrochemistry of the Iron-Molybdenum Cofactor of Nitrogenase Evidence for Multiple Speciation and Electrocatalytic Behavior... 

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