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dc.contributor.authorNath, Sunil
dc.contributor.authorJain, Siddhartha
dc.date.accessioned2005-06-27T10:51:03Z
dc.date.accessioned2019-02-09T07:12:20Z
dc.date.available2005-06-27T10:51:03Z
dc.date.available2019-02-09T07:12:20Z
dc.date.issued2000
dc.identifier.citationBiochemical and biophysical research communications, 272(3), 629-633en
dc.identifier.urihttp://localhost:8080/xmlui/handle/12345678/390
dc.description.abstractBased on the torsional mechanism of ATP synthesis by ATP synthase, a kinetic scheme has been developed in this work. The scheme considers adenine nucleotide transport, binding of substrates ADP and Pi, unbinding of product ATP, and ATP synthesis. This kinetic scheme has been analyzed mathematically, and a kinetic model has been obtained to explain the experimentally observed hyperbolic Michaellian dependence of the rate of ATP synthesis on the ADP concentration by ATP synthase under physiological steadystate operating conditions. The principal results of the kinetic model have been compared with the experimental data and an estimate of the enzymological kinetic parameters Vmax, KM, and KI has been determined.Mechanistic implications arising from further analysis of the kinetic model have been discussed. These biological implications provide deep insight into the sequence of events leading to ATP synthesis.en
dc.format.extent1298431 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoenen
dc.subjectATP synthaseen
dc.subjectF1F0en
dc.subjectkinetic modelen
dc.subjectmolecular mechanismen
dc.subjecttorsional mechanismen
dc.subjectkinetic parametersen
dc.subjectcompetitive inhibitionen
dc.subjectbiological implicationsen
dc.titleKinetic modeling of ATP synthesis by ATP synthase and Its mechanistic implicationsen
dc.typeArticleen


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