Summary
Some species of anoxygenic photosynthetic bacteria possess transhydrogenase and NADH dehydrogenase enzymes that are closely related to equivalent enzymes from animal mitochondria. Both are membrane proteins which couple redox reactions of the nicotinamide nucleotides to the translocation of hydrogen ions. Transhydrogenase catalyses the reversible transfer of reducing equivalents between NAD(H) and NADP(H); it has a low proton pumping stoichiometry. Probably under most conditions NADH dehydrogenase serves to transfer reducing equivalents from NADH to ubiquinone; it has a high proton pumping stoichiometry. Both enzymes are very active in chromatophore membranes isolated from cells of Rhodobacter and Rhodospirillum species grown anaerobically in the light, but their physiological function during phototrophic growth is not clear. Transhydrogenase may be involved in the transfer of reducing power between the cytoplasmic NAD(H) and NADP(H) pools, governed by the transmembrane proton electrochemical gradient (Δp), and in response to the metabolic needs of the cell. It might have a lesser role in the generation or regulation of Δp. During aerobic growth in the dark, NADH dehydrogenase undoubtedly serves as a major generator of Δp; during phototrophic growth it might be essential for the oxidation of highly reduced carbon substrates by auxiliary oxidants such as nitrate or dimethylsulfoxide, or it might be expressed in ‘readiness’ for the return to dark aerobic growth.
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Jackson, J.B. (1995). Proton-Translocating Transhydrogenase and NADH Dehydrogenase in Anoxygenic Photosynthetic Bacteria. In: Blankenship, R.E., Madigan, M.T., Bauer, C.E. (eds) Anoxygenic Photosynthetic Bacteria. Advances in Photosynthesis and Respiration, vol 2. Springer, Dordrecht. https://doi.org/10.1007/0-306-47954-0_38
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