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Titlebook: Nitrogen Fixation: Fundamentals and Applications; Proceedings of the 1 Igor A. Tikhonovich,Nikolai A. Provorov,William E. Conference procee

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Probing Catalytic Function through Amino-Acid Substitutions in , Molybdenum-Dependent Nitrogenaseenase), we are attempting to map the catalytic surface of both the FeMo-cofactor (FeMoco) and the P-cluster pair by individually substituting amino-acid residues within their polypeptide environments and analyzing the catalytic, redox and spectroscopic consequences for the resulting altered MoFe pro
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ATP Hydrolysis and Energy Transduction by Nitrogenasecomponent proteins (the Fe-protein and the MoFe-protein), reductant dithionite, substrates and products (Lowe, Thorneley, 1984a,b; Thorneley, Lowe, 1983, 1984a,b). In this cycle ATP hydrolysis is associated with electron transfer from Kp2 to Kpl followed by obligate, rate-limiting, dissociation of t
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Nitrogenase and Its Chemical Modelspolynuclear complex. Apparently, this arrangement corresponds to the maximum activation of dinitrogen and leads to the possibility of using comparatively weak reducing agents. Although there is no evidence for direct interaction of N. with iron atoms in cofactor, this is very likely, while vanadium
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978-94-010-4170-6Kluwer Academic Publishers 1995
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