Evidence for Changes in the Nucleotide Conformation in the Active Site of H+-ATPase As Determined by Pulsed EPR Spectroscopy
Author:
Affiliation:
1. CEA/Saclay, Département de Biologie Cellulaire et Moléculaire, Section de Bioénergétique, Bât. 532, F-91191 Gif-sur-Yvette, France, and Department of Biology and Geosciences, Shizuoka University, Shizuoka 422-8529, Japan
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi0014599
Reference57 articles.
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2. Pulse EPR of Paramagnetic Centers in Solid Phases;Progress in Theoretical Chemistry and Physics;2012-09-13
3. 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
4. Conformational Role of the Divalent Metal in Bovine Heart Mitochondrial F1-ATPase: An Electron Spin Echo Envelope Modulation Study;Biochemistry;2007-10-26
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