The NT-26 cytochrome c552 and its role in arsenite oxidation |
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Authors: | Joanne M Santini Ulrike Kappler Michael J Honeychurch Paul V Bernhardt |
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Institution: | a Department of Biology, UCL, Gower Street London WC1E 6BT, UK b School of Molecular and Microbial Sciences, Centre for Metals in Biology, The University of Queensland, 4072 Queensland, Australia c Department of Microbiology, La Trobe University, 3086 Victoria, Australia |
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Abstract: | Arsenite oxidation by the facultative chemolithoautotroph NT-26 involves a periplasmic arsenite oxidase. This enzyme is the first component of an electron transport chain which leads to reduction of oxygen to water and the generation of ATP. Involved in this pathway is a periplasmic c-type cytochrome that can act as an electron acceptor to the arsenite oxidase. We identified the gene that encodes this protein downstream of the arsenite oxidase genes (aroBA). This protein, a cytochrome c552, is similar to a number of c-type cytochromes from the α-Proteobacteria and mitochondria. It was therefore not surprising that horse heart cytochrome c could also serve, in vitro, as an alternative electron acceptor for the arsenite oxidase. Purification and characterisation of the c552 revealed the presence of a single heme per protein and that the heme redox potential is similar to that of mitochondrial c-type cytochromes. Expression studies revealed that synthesis of the cytochrome c gene was not dependent on arsenite as was found to be the case for expression of aroBA. |
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Keywords: | Arsenite oxidation Metabolism Cytochrome Redox potential |
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