Evaluation by steady-state enzyme kinetics of the role of tightly bound nucleotides during photophosphorylation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology
Link
http://link.springer.com/content/pdf/10.1007/BF00744524.pdf
Reference33 articles.
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3. Bar-Zvi, D., and Shavit, N. (1980). Role of tight nucleotide binding in the regulation of the chloroplast ATP synthetase activities,FEBS Lett. 119, 68?72.
4. Bar-Zvi, D., and Shavit, N. (1982). Modulation of the chloroplast ATPase by tight binding of nucleotides,Biochim. Biophys. Acta 681, 451?458.
5. Bennun, A., and Avron, M. (1965). The relation of the light-dependent and light-triggered adenosine triphosphatases to photophosphorylation,Biochim. Biophys. Acta 109, 117?127.
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1. The binding change mechanism for ATP synthase — Some probabilities and possibilities;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1993-01
2. Photophosphorylation at variable ADP concentration but constant ΔpH in lettuce thylakoids;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1989-04
3. Phosphorylation as explosive reaction;Biochemical Society Transactions;1987-12-01
4. Steady-state kinetics of ADP-arsenate and ATP-synthesis in Rhodospirillum rubrum chromatophores;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1984-07
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