tailieunhanh - Báo cáo khoa học: Enzymatic and electron paramagnetic resonance studies of anabolic pyruvate synthesis by pyruvate: ferredoxin oxidoreductase from Hydrogenobacter thermophilus

Pyruvate: ferredoxin oxidoreductase (POR; EC ) catalyzes the thia-mine pyrophosphate-dependent oxidative decarboxylation of pyruvate to form acetyl-CoA and CO2 . The thermophilic, obligate chemolithoauto-trophic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilusTK-6, assimilates CO2 via the reductive tricarboxylic acid cycle. | ỊFEBS Journal Enzymatic and electron paramagnetic resonance studies of anabolic pyruvate synthesis by pyruvate ferredoxin oxidoreductase from Hydrogenobacter thermophilus Takeshi Ikeda1 z Masahiro Yamamoto1 Hiroyuki Arai1 Daijiro Ohmori2 Masaharu Ishii1 and Yasuo Igarashi1 1 Department of Biotechnology Graduate Schoolof Agriculturaland Life Sciences The University of Tokyo Japan 2 Department of Chemistry Schoolof Medicine Juntendo University Chiba Japan Keywords Hydrogenobacter thermophilus iron-sulfur cluster pyruvate ferredoxin oxidoreductase reductive tricarboxylic acid cycle thiamine pyrophosphate Correspondence M. Ishii Department of Biotechnology Graduate School of Agricultural and Life Sciences The University of Tokyo 1-1-1 Yayoi Bunkyo-ku Tokyo 113-8657 Japan Fax 81 3 5841 5272 Tel 81 3 5841 5143 E-mail amishii@ Present address Research Institute for Nanodevice and Bio Systems Hiroshima University Japan - Institute of Biogeoscience Japan Agency for Marine-Earth Science and Technology JAMSTEC Kanagawa Japan Received 11 September 2009 revised 17 November 2009 accepted 19 November 2009 doi Pyruvate ferredoxin oxidoreductase POR EC catalyzes the thiamine pyrophosphate-dependent oxidative decarboxylation of pyruvate to form acetyl-CoA and CO2. The thermophilic obligate chemolithoauto-trophic hydrogen-oxidizing bacterium Hydrogenobacter thermophilus TK-6 assimilates CO2 via the reductive tricarboxylic acid cycle. In this cycle POR acts as pyruvate synthase catalyzing the reverse reaction . reductive carboxylation of acetyl-CoA to form pyruvate. The pyruvate synthesis reaction catalyzed by POR is an energetically unfavorable reaction and requires a strong reductant. Moreover the reducing equivalents must be supplied via its physiological electron mediator a small iron-sulfur protein ferredoxin. Therefore the reaction is difficult to demonstrate in vitro and the reaction mechanism has been poorly .

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