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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/387

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dc.contributor.authorJain, Siddhartha-
dc.contributor.authorNath, Sunil-
dc.date.accessioned2005-06-27T10:42:34Z-
dc.date.available2005-06-27T10:42:34Z-
dc.date.issued2000-
dc.identifier.citationFEBS letters, 476, 113-117en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/387-
dc.description.abstractAbstract Recently, a novel molecular mechanism of torque generation in the F0 portion of ATP synthase was proposed [Rohatgi, Saha and Nath (1998) Curr. Sci. 75, 716-718].In this mechanism, rotation of the c-subunit was conceived to take place in 12 discrete steps of 30³ each due to the binding and unbinding of protons to/from the leading and trailing Asp-61 residues of the c-subunit, respectively. Based on this molecular mechanism, a kinetic scheme has been developed in this work. The scheme considers proton transport driven by a concentration gradient of protons across the proton half-channels, and the rotation of the csubunit changes in the electrical potential only. This kinetic scheme has been analyzed mathematically and an expression has been obtained to explain the pH dependence of the rate of ATP synthesis by ATP synthase under steady state operating conditions. For a single set of three enzymological kinetic parameters, this expression predicts the rates of ATP synthesis which agree well with the experimental data over a wide range of pHin and pHout. A logical consequence of our analysis is that vpH and v iare kinetically inequivalent driving forces for ATP synthesis.en
dc.format.extent201272 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectATP synthaseen
dc.subjectKinetic modelen
dc.subjectTorqueen
dc.subjectpHen
dc.subjectElectrical potentialen
dc.subjectEnergy transductionen
dc.subjectInequivalenceen
dc.subjectKinetic parameteren
dc.titleKinetic model of ATP synthase: pH dependence of the rate of ATP synthesisen
dc.typeArticleen
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