Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I
نویسندگان
چکیده
منابع مشابه
Quinone binding and reduction by respiratory complex I.
Complex I (NADH:ubiquinone oxidoreductase) has a central function in oxidative phosphorylation and hence for efficient ATP production in most prokaryotic and eukaryotic cells. This huge membrane protein complex transfers electrons from NADH to ubiquinone and couples this exergonic redox reaction to endergonic proton pumping across bioenergetic membranes. Although quinone reduction seems to be c...
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The transfer of electrons and protons between membrane-bound respiratory complexes is facilitated by lipid-soluble redox-active quinone molecules (Q). This work presents a structural analysis of the quinone-binding site (Q-site) identified in succinate:ubiquinone oxidoreductase (SQR) from Escherichia coli. SQR, often referred to as Complex II or succinate dehydrogenase, is a functional member o...
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Complex I is a crucial respiratory enzyme that conserves the energy from NADH oxidation by ubiquinone-10 (Q10) in proton transport across a membrane. Studies of its energy transduction mechanism are hindered by the extreme hydrophobicity of Q10, and they have so far relied on native membranes with many components or on hydrophilic Q10 analogues that partition into membranes and undergo side rea...
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15 صفحه اولon semihypergroups and hypergroups
in this thesis, first the notion of weak mutual associativity (w.m.a.) and the necessary and sufficient condition for a $(l,gamma)$-associated hypersemigroup $(h, ast)$ derived from some family of $lesssim$-preordered semigroups to be a hypergroup, are given. second, by proving the fact that the concrete categories, semihypergroups and hypergroups have not free objects we will introduce t...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2017
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1714074114