Dependence of kinetic parameters of chloroplast ATP synthase on external pH, internal pH, and .DELTA.pH
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00242a007
Reference50 articles.
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2. Complete kinetic and thermodynamic characterization of the unisite catalytic pathway of Escherichia coli F1-ATPase. Comparison with mitochondrial F1-ATPase and application to the study of mutant enzymes.
3. A shift in chloroplast energy coupling by KCl from localized to bulk phase delocalized proton gradients
4. ΔpH-dependent activation of chloroplast coupling factors and external pH effects on the 9-aminoacridine response in lettuce and spinach thylakoids
5. ΔpH-activation of the thiol-modified chloroplast ATP hydrolase
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1. The Laboratory of Photosynthesis and its successors at Gif-sur-Yvette, France;Discoveries in Photosynthesis;2005
2. The laboratory of photosynthesis and its successors at Gif-sur-Yvette, France;Photosynthesis Research;2002
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4. The role of transmembrane electrochemical potential and phosphorylation of PS II proteins in temperature induced light emission from ATP-treated lettuce thylakoids;Photosynthesis Research;1996-03
5. The △pH-driven, ATP-independent Protein Translocation Mechanism in the Chloroplast Thylakoid Membrane;Journal of Biological Chemistry;1995-01
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