1. Molecular devices of chloroplast F1-ATP synthase for the regulation
- Author
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Heinrich Strotmann, Toru Hisabori, Hiroki Konno, Dirk Bald, and Hiroki Ichimura
- Subjects
γ subunit ,Light ,Rotation ,Protein Conformation ,Molecular Sequence Data ,Biophysics ,ε subunit ,Photophosphorylation ,Biology ,Chloroplast ,Biochemistry ,Electron Transport ,Adenosine Triphosphate ,ATP synthase gamma subunit ,F-ATPase ,Chloroplast Proton-Translocating ATPases ,V-ATPase ,Amino Acid Sequence ,Disulfides ,Photosynthesis ,ATP synthase ,Chemiosmosis ,food and beverages ,Cell Biology ,Electron transport chain ,Enzyme Activation ,Redox regulation ,biology.protein ,Protons ,Oxidation-Reduction ,Sequence Alignment ,ATP synthase alpha/beta subunits - Abstract
In chloroplasts, synthesis of ATP is energetically coupled with the utilization of a proton gradient formed by photosynthetic electron transport. The involved enzyme, the chloroplast ATP synthase, can potentially hydrolyze ATP when the magnitude of the transmembrane electrochemical potential difference of protons (DAH + ) is small, e.g. at low light intensity or in the dark. To prevent this wasteful consumption of ATP, the activity of chloroplast ATP synthase is regulated as the occasion may demand. As regulation systems DAH + activation, thiol modulation, tight binding of ADP and the role of the intrinsic inhibitory subunit q is well documented. In this article, we discuss recent progress in understanding of the regulation system of the chloroplast ATP synthase at the molecular level. D 2002 Elsevier Science B.V. All rights reserved.
- Published
- 2002
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