T chemiosmotic mechanisms of ATP synthesis is supported by strict mutual encoding of your complexes in genomes of Methanosarcinaceae members isolated from marine environments, exactly where Na -dependent ATP synthesis is really a dominant characteristic (46). Genomes of obligate H2-oxidizing CO2-reducing methanogens isolated from either marine or freshwater environments, incapable of acetotrophic or methylotrophic development, do not encode both Rnf and Mrp complexes (18, 39). These species are incapable of electron transport coupled to generation of ion gradients, negating the requirement for Rnf and Mrp complexes (48).Nature has evolved diverse Fd:CoM-S-S-CoB oxidoreductase systems in acetotrophic methanogens that generate ion gradients driving ATP synthesis that are various from M. acetivorans and don’t call for Rnf and Mrp complexes for development. Although M. barkeri and M. mazei make use of the development substrate acetate, the genomes of these freshwater species do not encode Rnf and Mrp complexes (49). As an alternative, unlike M acetivorans and also other marinedwelling members on the Methanosarcinaceae, M. barkeri and M. mazei are capable of metabolizing H2, which can be both produced and consumed in the oxidation of Fd and reduction of CoM-S-S-CoB for the duration of growth with acetate, yielding a theoretical five H (16). The H gradient coupled with two Na translocated by Mtr yields a theoretical ratio of two Na /5 H , when compared with 6 Na /2 H for M. acetivorans. Sadly, specificity for translocation of Na and H by the ATP synthase of M. barkeri and M. mazei has not been investigated. Methanosaeta spp. only use acetate as a growth substrate and usually do not metabolize H2 or encode Rnf and Mrp complexes, suggesting however yet another mechanism for producing ion gradients that drive ATP synthesis (50). Certainly, it’s proposed that Methanosaeta thermophila utilizes a Fd:CoM-S-S-CoB oxidoreductase system comprised of a truncated kind of F420H2 dehydrogenase and MP and that generates a H gradient driving ATP synthesis (51).ACKNOWLEDGMENTSThe work was supported by National Science Foundation grant number 0820734 to J.G.F., by the Person Endowment in the Pennsylvania State University to J.G.F., and in portion by grants from the U.S. Division ofjb.asm.orgJournal of BacteriologyMrp Complex in M. acetivoransEnergy, Workplace of Science, numbers DE-FG02-93ER20106 and DE-FG0207ER64502, to K.R.S.
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