Coordination of Nucleotides to Metals at the M2 and M3 Metal-Binding Sites of Spinach Chloroplast F1-ATPase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00199a025
Cited by 26 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
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2. Application of DFT methods to the study of the coordination environment of the VO2+ ion in V proteins;JBIC Journal of Biological Inorganic Chemistry;2012-04-15
3. Structural basis for VO2+-inhibition of nitrogenase activity: (B) pH-sensitive inner-sphere rearrangements in the 1H-environment of the metal coordination site of the nitrogenase Fe–protein identified by ENDOR spectroscopy;JBIC Journal of Biological Inorganic Chemistry;2008-04-02
4. Structural basis for VO2+ inhibition of nitrogenase activity (A): 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy;JBIC Journal of Biological Inorganic Chemistry;2008-03-20
5. Multiple Inequivalent Metal−Nucleotide Coordination Environments in the Presence of the VO2+-Inhibited Nitrogenase Iron Protein: pH-Dependent Structural Rearrangements at the Nucleotide Binding Site;Biochemistry;2002-10-11
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