Effects of l, N6-ethenoadenylates on the regulation of photosynthetic activities by adenylates; A study of the nucleotide binding sites on chloroplast coupling factor 1 |
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Authors: | Mukohata Yasuo; Sugiyama Yasuo |
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Institution: | Department of Biology, Faculty of Science, Osaka University Toyonaka 560, Japan |
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Abstract: | Effects of l, N6-ethenoadenylates (e-adenylates) were testedon phosphorylation, and electron transport under phosphorylation,arsenylation and quasi-arsenylation (stimulation of electrontransport in the presence of ATP, AMP and arsenate) conditionsin isolated spinach chloroplasts. -ATP as well as ATP partially inhibited ferricyanide reductionthrough binding to the chloroplast coupling factor 1 with anapparent dissociation constant (KDapp) of around 5µM,which was remarkably larger than that for ATP (ca. 2µM).e-ATP at below 500 µM had no effect on phosphorylationbut inhibited quasi-arsenylation in competition with ATP withan apparent inhibition constant (K1app) of around 60 µM. -ADP as well as ADP partially inhibited ferricyanide reductionwith a KDapp value close to that for -ATP. -ADP was phosphorylated(the apparent Michaelis constant, Kmapp=80µM) accompanyingstimulation of ferricyanide reduction to the magnitude predicted(P/ e=l). -ADP-arsenylation was also detected by stimulationof ferricyanide reduction. -AMP alone caused little inhibition of ferricyanide reductionas AMP, but competitively depressed the electron transport inhibitionby ADP and ATP with a K1app value of around 200 µM. -AMPwas not effective for ADP phosphorylation but inhibited stimulationdue to quasi-arsenylation coupling in competition with AMP K1app=150µM Among the possible combinations of adenylates and -adenylatesfor quasiarsenylation, only ATP+AMP] could couple with theenergy transduction mechanism. Based on the specificity of binding sites to adenylates and -adenylates, an attempt was made to distinguish at least four(two pairs) kinds of binding sites (at least six sites in toto)on the chloroplast coupling factor 1 for photosynthetic energytransduction. When one pair of sites is occupied by the designatedadenylates or -adenylates (allosteric effectors), the couplingfactor is thought to be in a conformation for coupling withthe energy transduction mechanism in the presence of phosphateor arsenate.
1Presented to the 1st Symposium of Japan Bioenergetics Group,December 19, 1975, Osaka. (Received February 17, 1976; ) |
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