Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus英文文献资料.docVIP

Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus英文文献资料.doc

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Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus英文文献资料

Archaea 1, 95–104 ? 2002 Heron Publishing—Victoria, Canada Cellular localization of D-lactate dehydrogenase and NADH oxidase fromArchaeoglobusfulgidus VISHWAJEETH REDDY PAGALA,1 JOOHYE PARK,1 DAVID W. REED1,2 and PATRICIA L. HARTZELL3,4 1 Department of Microbiology, Molecular Biology, and Biochemistry, University of Idaho, Moscow, ID 83844-3052, USA 2 Present address: Idaho National Engineering and Environmental Laboratories, Idaho Falls, ID 83415, USA 3 142 Life Science, University of Idaho, Moscow, ID 83844-3052, USA 4 Author to whom correspondence should be addressed (hartzell@) Received October 10, 2001; accepted February 5, 2002; published online March 6, 2002 Summary Members of the genus Archaeoglobus are hyper- ments, such as ocean and terrestrial oil deposits, where they likely account for the formation of H2S-contaminated “sour oil.” Both Archaeoglobus fulgidus and Caldivirga maquilin- gensis thrive at 85 °C, their optimal growth temperature (Stet- ter 1988, Itoh et al. 1999). The enzymes involved in sulfate reduction, ATP sulfurylase, adenylsulfate reductase and sulfite reductase, have been char- acterized in A. fulgidus (Speich et al. 1988, Dahl et al. 1990) and are similar to enzymes involved in sulfate reduction in mesophilic bacteria (Hansen 1994). During dissimilatory sul- fate reduction, sulfate is activated by ATP to form adenosyl- phosphosulfate (APS) (Hansen 1988). This reaction is catalyzed by ATP sulfurylase. Adenosylphosphosulfate is then thermophilic sulfate reducers with an optimal growth tempera- ture of 83 °C. Archaeoglobus fulgidus can utilize simple com- pounds including D-lactate, L-lactate and pyruvate as the sole substrate for carbon and electrons for dissimilatory sulfate re- duction. Previously we showed that this organism makes a D-lactate dehydrogenase (Dld) that requires FAD and Zn2+ for activity. To determine the cellular location and topology of Dld and to identify proteins that interact wi

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