Integrated functioning of the chloroplast coupling factor.
This review is focused on some functional characteristics of the chloroplast coupling factor. The structure of the enzyme and the putative role of its subunits are recalled. An attempt is made to discriminate the driving force and the activator effects of the electrochemical proton gradient. Respective roles of delta pH, delta phi, external and internal pH are discussed with regard to mechanistic implications. The hypothesis of a functional switch of the enzyme between two states with better efficiency either in ATP synthesis or in ATP hydrolysis is also examined. A brief survey is made on some problems complicating quantitative studies of energy coupling, such as localized chemiosmosis, delta pH and delta phi computations, and scalar ATPases. The main data on the enzyme activation and the energy-dependent release of tightly bound nucleotides are summarized. The arguments for and against the catalytic competence of theses nucleotides are reviewed. Lastly, some prevailing models of the catalytic mechanism are presented. The relevance of nucleotides binding change events in this process is discussed.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000378:metabolism; D002352:Carrier Proteins; D004563:Electrochemistry; D004579:Electron Transport; D004734:Energy Metabolism; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000502:physiology; D008970:Molecular Weight; D018521:Plant Physiological Phenomena; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000502:physiology*; D011522:Protons
D002352:Carrier Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D011522:Protons; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases