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Titlebook: Nitrogen Fixation; Achievements and Obj Peter M. Gresshoff,L. Evans Roth,William E. Newton Book 1990 Springer Science+Business Media Dordre

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Crystal structure of the nitrogenase iron protein from ,tion, electrons are transferred from Fe-protein to MoFe-protein in an ATP-dependent process. The coupling of ATP hydrolysis to electron transfer is mediated by Fe-protein, which is the only known reductant of MoFe-protein supporting catalytic activity (8). Fe-protein is a dimer of two identical 32kD
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Structure of the nitrogenase MoFe protein: Spatial distribution of the intrinsic metal atoms determiis of a series of EPR and Mössbauer experiments [1]. This model defined two types of metal-sulfur clusters, M-centers and P-clusters. The original and current versions of the model both identify the M-centers as FeMo-cofactors. Two are bound per α.β. tetramer; each comprises 1 Mo and 6–7 Fe atoms. P
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Vanadium nitrogenase of ,ptides of the enzyme. In this synthesis paper on V-nitrogenase we review material published since the International Nitrogen Fixation Congress in Cologne in 1988 and also discuss some of our unpublished data.
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