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