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Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium

Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium

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Prüfsumme: MD5:ea5fe07a6897bab5c6802501957e9040

FRIEDRICH, Michael, Bernhard SCHINK, 1993. Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium. In: FEBS European Journal of Biochemistry. 217(1), pp. 233-240. ISSN 0014-2956. eISSN 1432-1033

@article{Friedrich1993Hydro-6939, title={Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium}, year={1993}, doi={10.1111/j.1432-1033.1993.tb18238.x}, number={1}, volume={217}, issn={0014-2956}, journal={FEBS European Journal of Biochemistry}, pages={233--240}, author={Friedrich, Michael and Schink, Bernhard} }

Oxidation of glycolate to 2 CO, and 3 H, (AGO' = +36 kJ/mol glycolate) by the proton-reducing, glycolate-fermenting partner bacterium of a syntrophic coculture (strain FlGlyM) depends on a low hydrogen partial pressure (pH). The first reaction, glycolate oxidation to glyoxylate ( E O f = -92 mV) with protons as electron acceptors (Eo' = -414 mV), is in equilibrium only at a pH2 of 1 pPa which cannot be maintained by the syntrophic partner bacterium Methanospirillurn hungatei; energy therefore needs to be spent to drive this reaction. Glycolate dehydrogenase activity (0.3-0.96 U . mg protein-') was detected which reduced various artificial electron acceptors such as benzyl viologen, methylene blue, dichloroindophenol, K,[Fe(CN),], and water-soluble quinones.<br />Fractionation of crude cell extract of the glycolate-fermenting bacterium revealed that glycolate dchydrogcnase, hydrogenase, and proton-translocating ATPase were membrane-bound. Menaquinones wcre found as potential electron camers. Everted membrane vesicles of the glycolate-fermenting bacterium catalyzed ATP-dependent H, formation from glycolate (30-307 nmol H, - min-'.<br />mg protein-'). Protonophores, inhibitors of proton-translocating ATPase, and the quinone analog antimycin A inhibited H, formation from glycolate, indicating the involvement of proton-motive force to drive the endergonic oxidation of glycolate to glyoxylate with concomitant H, release. This is the first demonstration of a reversed electron transport in syntrophic interspecies hydrogen transfer. 1993 deposit-license First publ. in: FEBS European Journal of Biochemistry 217 (1993), 1, pp. 233-240 Schink, Bernhard application/pdf Friedrich, Michael Friedrich, Michael Schink, Bernhard 2011-03-24T17:30:17Z eng Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium 2011-03-24T17:30:17Z

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