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Carboxydothermus hydrogenoformans

Parkin A, Seravalh J, Vincent KA, Ragsdale SW, Armstrong FA. 2007. Rapid and efficient elec-trocatal3tic CO2/CO interconversions by Carboxydothermus hydrogenoformans CO dehydrogenase I on an electrode. J Am Chem Soc 129 10328-10329. [Pg.633]

Svetlitchnyi, V., Dobbek, H., Meyer-Klauke, W., Meins, T., Thiele, B., Romer, P., Huber, R. and Meyer, O. (2004) A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans, Proc. Natl. Acad. Sci. U.S.A., 101, 446-451. [Pg.269]

Carbon monoxide dehydrogenase/acetyl coenzyme A synthase (CODH/ACS) describes two different classes of enzymes carbon monoxide dehydrogenase (CODH) isolated from Rhodospirillum rubrum or Carboxydothermus hydrogenoformans reversibly oxidizes CO to CO2 according to equation (2), and the bifunctional CODH/ACS enzyme from Moorella thermoacetica catalyzes the reversible reduction of CO2 to CO (CODH) and acetyl coenzyme assembly/disassembly (ACS) (equation 3). ... [Pg.2898]

C. therm, polymerase isolated from Carboxydothermus hydrogenoformans is a magnesium-dependent enzyme with both reverse transcriptase and DNA polymerase activities. C. therm, polymerase has a short half-life at 95 °C and Taq polymerase can be added to the reaction to improve the amplification. [Pg.112]

Svetlitchnyi V, Peschel C, Acker G, Meyer O (2001) Two membrane-associated [NiFeS]-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacte-rium Carboxydothermus hydrogenoformans. J Bacteriol 183 5134-5144. doi 10.1128/jb.l83. 17.5134-5144.2001... [Pg.263]


See other pages where Carboxydothermus hydrogenoformans is mentioned: [Pg.183]    [Pg.261]    [Pg.32]    [Pg.2303]    [Pg.2850]    [Pg.3929]    [Pg.2849]    [Pg.699]    [Pg.889]    [Pg.362]    [Pg.183]    [Pg.261]    [Pg.32]    [Pg.2303]    [Pg.2850]    [Pg.3929]    [Pg.2849]    [Pg.699]    [Pg.889]    [Pg.362]    [Pg.63]   
See also in sourсe #XX -- [ Pg.261 ]

See also in sourсe #XX -- [ Pg.32 ]




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