THE STRUCTURE OF SOXAX: A CYTOCHROME WITH A ROLE IN THIOSULFATE OXIDATION

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Reduced sulfur compounds can be used a electron donors by a variety of microorganisms, supporting autotrophic growth. Thiosulfate is one of the most abundant forms of reduced sulfur in Nature, and the ability to oxidise this compound is found in many microorganisms. The best studied pathway of thiosulfate oxidation involves the thiosulfate-oxidising multi-enzyme system (TOMES) which can oxidise thiosulfate, sulfite or sulfide to sulfate with cytochrome c as the electron acceptor. This pathway is encoded by sulfur oxidation (sox) gene clusters and contains heme proteins (SoxB, SoxC) as well as a number of cytochromes (SoxA, SoxX, SoxD, SoxE). SoxAX is heterodimeric protein with two heme c-bearing subunits of approximately 30 and 15 kDa, respectively. The SoxAX to be studied here is that from Starkeya novell