Correlation between the ATP synthetic active state and the ATP hydrolytic active state in chloroplast ATP synthase-ATPase complex CF0 . CF1.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
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Cited by 5 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. Energy-dependent changes in the conformation of the chloroplast ATP synthase and its catalytic activity;European Journal of Biochemistry;1993-06
2. Energy-dependent changes in conformation and catalytic activity of the chloroplast ATP synthase.;Journal of Biological Chemistry;1992-02
3. Energy-dependent Conformational Changes in the ϵ Subunit of the Chloroplast ATP Synthase (CF0CF1);Journal of Biological Chemistry;1989-10
4. Studies on well-coupled Photosystem I-enriched subchloroplast vesicles — energy-dependent switching between two different active states of the proton-translocation adenosine triphosphatase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1988-12
5. Glucose permease of Escherichia coli. The effect of cysteine to serine mutations on the function, stability, and regulation of transport and phosphorylation.;Journal of Biological Chemistry;1988-05
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