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SilhouetteFxV5Crack( 6.1.17) · NEW UPDATE 1.3.5 · This is fully patched and tested program. .NADPH, ubiquinone and succinate-dependent electron transfer in the membrane-bound methyl-coenzyme M hydrogenase.
The electron flow from succinate to methyl-coenzyme M in the membrane-bound methyl-coenzyme M hydrogenase of Escherichia coli is shown to be coupled to the reduction of both quinone and pyridine nucleotide. The NAD(P)H-dependent electron transfer activity was significantly affected by both succinate and oxidized methyl-coenzyme M; both reaction products blocked the electron transfer activity in the membrane, whereas methyl-coenzyme M reduced to methyl-reduced methyl-coenzyme M stimulated it. Membrane vesicles containing 3-[4-pyrenyl]-2,2,3-trimethyl-3H-indolium, a potent inhibitor of the quinone reduction activity of the membrane-bound hydrogenase, did not contain detectable electron transport activity between succinate and methyl-coenzyme M. The results suggest that the primary electron flow from succinate to the membrane-bound methyl-coenzyme M hydrogenase is via NAD(P)H and that the electron flow from methyl-coenzyme M to ubiquinone may take place via methyl-coenzyme M-quinone reductase.function f(n) {
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