AbstractAn early proposal was that for rapid ATP synthesis by the rotational ATP synthase, a specific second site must bind ADP and Pi, and for rapid ATP hydrolysis a different second site must bind ATP. Such bi-site activation was considered to occur whether or not an ADP or ATP was at a third site. In contrast, a more recent proposal is that rapid ATP hydrolysis requires that all three sites have bound ADP or ATP present. However, discovery that one second site binds ADP better than ATP, together with other data and considerations support the earlier proposal. The retention or rebinding of ADP can explain why three sites fill during hydrolysis as ATP concentration is increased although bi-site activation still prevails
AbstractPreincubation of submitochondrial particles with ADP in the presence of Mg2+ results in the ...
AbstractThe effect of inorganic phosphate (Pi) on uni-site ATP binding and hydrolysis by the nucleot...
AbstractUnder conditions of molar excess of enzyme, isolated F1-ATPase from beef heart mitochondria ...
AbstractAn early proposal was that for rapid ATP synthesis by the rotational ATP synthase, a specifi...
AbstractA suggested minimal scheme for substrate binding by and interconversion of three forms of th...
AbstractF1-ATPase is a rotary molecular motor in which the central γ subunit rotates inside a cylind...
AbstractIn ATP synthase, X-ray structures, demonstration of ATP-driven γ-subunit rotation, and trypt...
AbstractDuring ATP synthesis, ATP synthase has to bind MgADP in the presence of an excess of MgATP. ...
During ATP synthesis, ATP synthase has to bind MgADP in the presence of an excess of MgATP. Thus, fo...
AbstractIn active MF1, one of the two non-exchangeable tightly bound adenine nucleotides is an ATP, ...
Despite exhaustive chemical and crystal structure studies, the mechanistic details of how F o F 1 -A...
AbstractThe binding of one ADP molecule at the catalytic site of the nucleotide depleted F1-ATPase r...
Computer-designed artificial enzymes will require precise understanding of how conformation of activ...
AbstractNucleotide binding to nucleotide-depleted F1-ATPase from Escherichia coli (EcF1) during MgAT...
AbstractThe proton translocating ATP-synthase from chloroplasts, CF0F1, was isolated and reconstitut...
AbstractPreincubation of submitochondrial particles with ADP in the presence of Mg2+ results in the ...
AbstractThe effect of inorganic phosphate (Pi) on uni-site ATP binding and hydrolysis by the nucleot...
AbstractUnder conditions of molar excess of enzyme, isolated F1-ATPase from beef heart mitochondria ...
AbstractAn early proposal was that for rapid ATP synthesis by the rotational ATP synthase, a specifi...
AbstractA suggested minimal scheme for substrate binding by and interconversion of three forms of th...
AbstractF1-ATPase is a rotary molecular motor in which the central γ subunit rotates inside a cylind...
AbstractIn ATP synthase, X-ray structures, demonstration of ATP-driven γ-subunit rotation, and trypt...
AbstractDuring ATP synthesis, ATP synthase has to bind MgADP in the presence of an excess of MgATP. ...
During ATP synthesis, ATP synthase has to bind MgADP in the presence of an excess of MgATP. Thus, fo...
AbstractIn active MF1, one of the two non-exchangeable tightly bound adenine nucleotides is an ATP, ...
Despite exhaustive chemical and crystal structure studies, the mechanistic details of how F o F 1 -A...
AbstractThe binding of one ADP molecule at the catalytic site of the nucleotide depleted F1-ATPase r...
Computer-designed artificial enzymes will require precise understanding of how conformation of activ...
AbstractNucleotide binding to nucleotide-depleted F1-ATPase from Escherichia coli (EcF1) during MgAT...
AbstractThe proton translocating ATP-synthase from chloroplasts, CF0F1, was isolated and reconstitut...
AbstractPreincubation of submitochondrial particles with ADP in the presence of Mg2+ results in the ...
AbstractThe effect of inorganic phosphate (Pi) on uni-site ATP binding and hydrolysis by the nucleot...
AbstractUnder conditions of molar excess of enzyme, isolated F1-ATPase from beef heart mitochondria ...