Linked Life Data

18628203

Source:http://linkedlifedata.com/resource/pubmed/id/18628203

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pubmed-article:18628203pubmed:dateCreated2008-9-15lld:pubmed
pubmed-article:18628203pubmed:abstractTextThe F(0)F(1)-ATP synthase couples the functions of H(+) transport and ATP synthesis/hydrolysis through the efficient transmission of energy mediated by rotation of the centrally located gamma, epsilon, and c subunits. To understand the gamma subunit role in the catalytic mechanism, we previously determined the partial rate constants and devised a minimal kinetic model for the rotational hydrolytic mode of the F(1)-ATPase enzyme that uniquely fits the pre-steady state and steady state data ( Baylis Scanlon, J. A., Al-Shawi, M. K., Le, N. P., and Nakamoto, R. K. (2007) Biochemistry 46, 8785-8797 ). Here we directly test the model using two single cysteine mutants, betaD380C and betaE381C, which can be used to reversibly inhibit rotation upon formation of a cross-link with the conserved gammaCys-87. In the pre-steady state, the gamma-beta cross-linked enzyme at high Mg.ATP conditions retained the burst of hydrolysis but was not able to release P(i). These data show that the rate-limiting rotation step, k(gamma), occurs after hydrolysis and before P(i) release. This analysis provides additional insights into how the enzyme achieves efficient coupling and implicates the betaGlu-381 residue for proper formation of the rate-limiting transition state involving gamma subunit rotation.lld:pubmed
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pubmed-article:18628203pubmed:authorpubmed-author:Al-ShawiMarwa...lld:pubmed
pubmed-article:18628203pubmed:authorpubmed-author:NakamotoRober...lld:pubmed
pubmed-article:18628203pubmed:authorpubmed-author:ScanlonJoanne...lld:pubmed
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