Why R-Homocitrate Is Essential to the Reactivity of FeMo-Cofactor of Nitrogenase: Studies on NifV--Extracted FeMo-Cofactor
作者： Karin L. C. Grönberg , Carol A. Gormal , Marcus C. Durrant , Barry E. Smith , Richard A. Henderson
DOI: 10.1021/JA981832O
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摘要: The dinitrogen-binding site in the Mo-based nitrogenase is FeMo-cofactor, a metallo-sulfur cluster of composition MoFe7S9·R-homocitrate. NifV- mutant from Klebsiella pneumoniae contains an FeMo-cofactor which homocitrate has been replaced by citrate (i.e., MoFe7S9·citrate). Both wild type and cofactors (in S = 3/2 spin state) can be extracted into N-methylformamide. bind one molecule PhS- at tetrahedral Fe, rate this reaction depends on what else coordinated to cluster. No differences were observed between reactivities wild-type with when they complexed CN-, N3-, or H+. However, imidazole bound, kinetics reactions two are very different. Here we propose that R-homocitrate (but not citrate) hydrogen bond ligand Mo, perturbs electron distribution within core, hence its reactivity wi...
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