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Murataliev, M B; Boyer, P D (1994) Interaction of mitochondrial F1-ATPase with trinitrophenyl derivatives of ATP and ADP. Participation of third catalytic site and role of Mg2+ in enzyme inactivation. J Biol Chem 269:15431-9
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Boyer, P D (1993) The binding change mechanism for ATP synthase--some probabilities and possibilities. Biochim Biophys Acta 1140:215-50
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Zhou, J M; Boyer, P D (1993) Evidence that energization of the chloroplast ATP synthase favors ATP formation at the tight binding catalytic site and increases the affinity for ADP at another catalytic site. J Biol Chem 268:1531-8
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Zhou, J M; Boyer, P D (1992) MgADP and free Pi as the substrates and the Mg2+ requirement for photophosphorylation. Biochemistry 31:3166-71
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Murataliev, M B; Boyer, P D (1992) The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding. Acceleration of the ATP-dependent release of inhibitory ADP from a catalytic site. Eur J Biochem 209:681-7
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Murataliev, M B; Milgrom, Y M; Boyer, P D (1991) Characteristics of the combination of inhibitory Mg2+ and azide with the F1 ATPase from chloroplasts. Biochemistry 30:8305-10
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Milgrom, Y M (1991) When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites. Eur J Biochem 200:789-95
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Berkich, D A; Williams, G D; Masiakos, P T et al. (1991) Rates of various reactions catalyzed by ATP synthase as related to the mechanism of ATP synthesis. J Biol Chem 266:123-9
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Milgrom, Y M; Ehler, L L; Boyer, P D (1991) The characteristics and effect on catalysis of nucleotide binding to noncatalytic sites of chloroplast F1-ATPase. J Biol Chem 266:11551-8
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Milgrom, Y M; Boyer, P D (1990) The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site. Biochim Biophys Acta 1020:43-8
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