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- W1983802034 abstract "An increasing number of strict anaerobic bacteria are being found which use an alternative pathway to the ubiquitous Calvin cycle for CO2 fixation into cell compounds and the ubiquitous Krebs cycle for acetyl CoA oxidation to CO2. The principles of this non-cyclic pathway, the acetyl CoA pathway, have long been studied in acetogenic bacteria. These bacteria can catalyze the exergonic reduction of 2 CO2 with 8 reducing equivalents to acetate. In this pathway, CO2 reduction is part of a catabolic redox process which functions to accept reducing equivalents from a variety of dehydrogenated substrates. This process yields net ATP generated by electron transport phosphorylation. Acetyl CoA is an intermediate, formed from one CO2 via a tetrahydropteridine-bound 1-carbon unit (methyl group of acetate), and from another CO2 via a bound carbon monoxide (carboxyl group of acetate). The most characteristic and complex enzyme involved in acetyl CoA synthesis is carbon monoxide dehydrogenase (‘acetyl CoA synthase’). The enzymes of this acetyl CoA pathway not only participate in (1) acetate synthesis in energy metabolism of acetogenic bacteria, but also mediate (2) acetyl CoA oxidation in sulfate-reducing bacteria and possibly other anaerobes; (3) acetate disproportionation to CO2 and CH4 in the energy metabolism of many methanogenic bacteria; (4) autotrophic CO2 fixation in autotrophic acetogenic, methanogenic, and most autotrophic sulfate-reducing bacteria; (5) assimilation and/or dissimilation of 1-carbon compounds in many anaerobes; (6) CO oxidation to CO2 in anaerobes. A specialized group of anaerobes performs acetate synthesis from CO2 or from C1 units via a different pathway, the glycine synthase/glycine reductase pathway. Glycine is an intermediate which is formed from 2 C1 compounds, and is then reduced to acetate. The principal features of the two pathways and some open questions are discussed in this review. Emphasis is placed upon the acetyl CoA pathway in acetogenic bacteria, but important advances in the study of other strict anaerobes are also considered." @default.
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- W1983802034 date "1962-12-01" @default.
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- W1983802034 title "Enzymic oxidation of carbon monoxide III. Reversibility" @default.
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- W1983802034 doi "https://doi.org/10.1016/0006-3002(62)90454-7" @default.
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