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Results 1 - 6 of 6
EC Number General Information Commentary Reference
Display the reaction diagram Show all sequences 1.5.7.2evolution evolutionary trajectory of these oxidoreductases from a proton-reducing ancestral respiratory complex (ARC), overview. The diversification of ARC to membrane-bound hydrogenase (MBH), archaeal respiratory complex (MBX), FPO and eventually NADH quinone oxidoreductase (NUO) was driven by the larger energy yields associated with coupling ferredoxin oxidation to the reduction of oxidants with increasing electrochemical potential, including protons, SĀ° and membrane soluble organic compounds such as phenazines and quinone derivatives. Phylogenetic tree. Homology between the subunits of FPOF and FPOC with those in MBX and MBH. Evolution of FPO, detailed overview. FPO is now present only in strictly anaerobic, acetate-utilizing and sulfate-reducing archaea 741987
Display the reaction diagram Show all sequences 1.5.7.2metabolism model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during coculture with Geobacter metallireducens. Each two moles of ethanol oxidized to acetate by G. metallireducens releases eight electrons and eight protons. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo. Proton translocation drives Fpo-catalyzed reduction of F420 to F420H2. Half of the F420H2 produced serves as a reductant in the carbon dioxide reduction pathway. The remaining F420H2 is the electron donor for HdrABC, which reduces ferredoxin and CoM-S-S-CoB in an electron bifurcation reaction -, 764762
Display the reaction diagram Show all sequences 1.5.7.2more FPO demonstrates the flexible nature of the ARC-related complexes with respect to electron input and energetics reflected by differences in redox carriers and number of ions translocated 741987
Display the reaction diagram Show all sequences 1.5.7.2physiological function presence of an intersubunit electron transport pathway in heterodisulfide reductase HdrA2B2C2 dependent on ferredoxin or coenzyme F420 (F420H2) as an electron donor. HdrA2B2C2 catalyzes a thermodynamically favorable, flavin-based, coupling of the endergonic one-electron reduction of ferredoxin (E0 of ca. -520 mV) with F420H2 (E0 of -380 mV) to the exergonic reduction of CoMS-SCoB (E0 of -140 mV) -, 743210
Display the reaction diagram Show all sequences 1.5.7.2physiological function the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420 741987
Display the reaction diagram Show all sequences 1.5.7.2physiological function the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420. The FPO complex is mainly found in acetate-utilizing, methane-producing anaerobic Archaea where it functions to reduce the membrane-associated cofactor methanophenazine using either ferredoxin or the cytoplasmic cofactor F420 741987
Results 1 - 6 of 6