Determination of ligand binding constants for the iron-molybdenum cofactor of nitrogenase: monomers, multimers, and cooperative behavior
Author:
Publisher
Springer Science and Business Media LLC
Subject
Inorganic Chemistry,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s007750100247.pdf
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Evidence for a Metal−Thiolate Intermediate in Alkyl Group Transfer from Epoxypropane to Coenzyme M and Cooperative Metal Ion Binding in Epoxyalkane:CoM Transferase;Biochemistry;2005-09-10
2. Cooperativity and intermediates in the equilibrium reactions of Fe(II,III) with ethanethiolate in N-methylformamide solution;JBIC Journal of Biological Inorganic Chemistry;2005-04-29
3. Chemical Models, Theoretical Calculations, and the Reactivity of Isolated Iron-Molybdenum Cofactor;Catalysts for Nitrogen Fixation;2004
4. Binding Sites of Nitrogenase: Kinetic and Theoretical Studies of Cyanide Binding to Extracted FeMo-Cofactor Derivatives;Inorganic Chemistry;2003-09-03
5. Electron-Transfer Chemistry of the Iron–Molybdenum Cofactor of Nitrogenase: Delocalized and Localized Reduced States of FeMoco which Allow Binding of Carbon Monoxide to Iron and Molybdenum;Chemistry - A European Journal;2003-01-03
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