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- W2035264906 abstract "Abstract 1. The nitrite oxidase particles obtained by sonic oscillation of Nitrobacter agilis cells also possessed appreciable formate oxidase activity, ranging from about 25 to 50% of the nitrite oxidase activity depending upon the N. agilis strain. Both activities distributed themselves in the same pattern and proportions during differential centrifugation, and resided solely in the pellet resulting from high-speed centrifugation. 2. Difference spectra of formate-reduced particles or intact cells demonstrated the presence of cytochromes of the c - and a -types like those of the NO 2 − -reduced material. Under anaerobic conditions NO 3 − or fumarate acted as an alternate electron acceptor in place of O 2 in formate oxidation. Under aerobic conditions increasing NO 3 − concentrations resulted in (a) an increased role of NO 3 − as a terminal electron acceptor compared to O 2 , (b) a greater total enzymatic transfer of electrons from formate than if O 2 were the sole electron acceptor, and (c) a partial inhibition of O 2 uptake suggestive of a competition for electrons by the two acceptors. The formate oxidase system failed to catalyze consistently the transfer of electrons to either added mammalian cytochrome c or Fe(CN) 6 3− . The marked sensitivity of the system to certain inhibitors implicated cytochrome oxidase as an integral part of the formate oxidase. The system was also inhibited significantly by a variety of chelating agents, indicating a metal component in the formate dehydrogenase or early portion of the electron transfer sequence. 3. The stoichiometry of the formate oxidase system was shown to approach the theoretical value of 2 moles of CO 2 evolved per mole of O 2 or per 2 moles of formate consumed. 4. To a limited extent, phosphorylation occurred concomittantly with the oxidation of formate in the presence of the cell-free particulate system." @default.
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- W2035264906 title "Particulate formate oxidase from Nitrobacter agilis" @default.
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- W2035264906 doi "https://doi.org/10.1016/0005-2728(70)90108-8" @default.
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