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Showing 1 to 7 of 7 for “"quinone binding site"”.
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Biochemical characterization of a-type heme-copper oxidases in escherichia coli, bacillus subtilis and thermus thermophilus
… delivering protons either to active site for oxygen reduction or to proton loading site for pumping. However, a growing number of oxidases that lack this key glutamate and instead are replaced by a tyrosine-serine (YS) pair in proximity have been discovered and classified as A2-type …
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The interactions of cytochrome bo3 from Escherichia coli with its substrates - ubiquinone and oxygen
… enzyme contain between 0 to 2 equivalents of ubiquinone-8. Studies using ubiquinol-1, a soluble quinol substrate, indicate one high affinity quinone binding site, which acts as a non-exchanging co-factor, and a second, low-affinity site which is the substrate site. The residues interacting with …
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Computer simulation of titration behavior in proteins
… to the continuum electrostatics-based multiple site titration theory based on solvent accessibility is proposed, and it is shown that this model results in improved agreement of calculated pK$\rm\sb{a}$ values with experiment when a low protein interior dielectric constant is used. The …
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Interfacial modulation of protein function explored through atomistic molecular dynamics simulation
… bilayers. Separately, simulations of C2 domain binding of synaptogamin (Syt) to the HMMM demonstrate clear differences in the binding properties between Syt isoforms, and explain the atomic origins of the observed differential kinetics between Syt-1 and Syt-7. Development of the HMMM to extend …
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Structural and functional studies of mitochondrial NADH:ubiquinone oxidoreductase (complex I)
NADH:ubiquinone oxidoreductase (complex I) is the largest and most complicated enzyme in the mitochondrial electron transfer chain. It catalyses the oxidation of NADH and the reduction of ubiquinone, coupled to the translocation of protons across the mitochondrial inner membrane, maintaining the …
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Studies on assembly and genetic variation in mitochondrial respiratory complex I
Complex I (NADH:ubiquinone oxidoreductase) couples electron transfer to proton translocation across the inner mitochondrial membrane, to drive the synthesis of ATP. Its distinctive L-shaped structure comprises 45 subunits, encoded by both the mitochondrial and nuclear genomes, which are assembled …
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EPR and solid-state NMR studies on the mechanism of cytochrome bo3 ubiquinol oxidase from escherichia coli
… the ubiquinol pool are first transferred to a ubiquinone cofactor bound at the high affinity binding site known as the QH-site, from which electrons are moved one at a time sequentially to the low-spin heme b and the CuB-heme o3 catalytic site. In this study, E. coli C43(DE3) auxotroph strains …