Two membrane-boundb-type cytochromes inNitrosomonas europaea
نویسندگان
چکیده
منابع مشابه
CO-binding c-type cytochromes and a high-potential cytochrome c in Nitrosomonas europaea.
The purification of two soluble CO-binding cytochromes c from Nitrosomonas europaea is described. Cytochrome cCO-550 ran on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis with an apparent Mr of 32 000, whereas for cytochrome cCO-552 the apparent Mr was 16 000. Redox potentials (Em, 7) were determined as +140 and -50mV respectively. Cytochrome cCO-550 was co-purified with a cytochrom...
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A pigment-protein complex can be extracted, in aqueous 2-percent digitonin, from Euglena grown in the light. When further fractionated by acetone and ammonium sulfate this flagellate yields a c-type cytochrome. By similar extraction of dark-grown, nonphotosynthetic Euglena, another c-type cytochrome can be isolated. The cytochrome from the light-grown Euglena- is like that of cytochrome c isola...
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We demonstrate that the cccB gene, identified in the Bacillus subtilis genome sequence project, is the structural gene for a 10-kDa membrane-bound cytochrome c(551) lipoprotein described for the first time in B. subtilis. Apparently, CccB corresponds to cytochrome c(551) of the thermophilic bacterium Bacillus PS3. The heme domain of B. subtilis cytochrome c(551) is very similar to that of cytoc...
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Previous studies failed to detect c-type cytochromes in Pelobacter species despite the fact that other close relatives in the Geobacteraceae, such as Geobacter and Desulfuromonas species, have abundant c-type cytochromes. Analysis of the recently completed genome sequence of Pelobacter carbinolicus revealed 14 open reading frames that could encode c-type cytochromes. Transcripts for all but one...
متن کاملCyc2p, a membrane-bound flavoprotein involved in the maturation of mitochondrial c-type cytochromes.
Mitochondrial apocytochrome c and c1 are converted to their holoforms in the intermembrane space by attachment of heme to the cysteines of the CXXCH motif through the activity of assembly factors cytochrome c heme lyase and cytochrome c1 heme lyase (CCHL and CC1HL). The maintenance of apocytochrome sulfhydryls and heme substrates in a reduced state is critical for the ligation of heme. Factors ...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1983
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1983.tb00140.x