Purification and spectral characterization of a b-type cytochrome from the plasma membrane of the archaebacterium Sulfolobus acidocaldarius.
For the first time the purification of a heme-b containing cytochrome from the plasma membrane of an extremely thermoacidophilic archaebacterium is described. The detergent solubilized 30 kDa polypeptide contains two heme-b centers and one copper ion. According to its low temperature spectra and CO-binding properties, it is likely to function as a cytochrome-o like terminal oxidase in the membrane. The purified cytochrome does not retain catalytic activity, however.
Institute of Biochemistry, Medical University of Lübeck, Germany.
M
M
Becker
G
G
Schäfer
D002462:Cell Membrane / Q000201:enzymology; D002845:Chromatography; D003573:Cytochrome b Group / Q000737:chemistry / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D013054:Spectrophotometry, Atomic; D016945:Sulfolobus acidocaldarius / Q000201:enzymology*
D003573:Cytochrome b Group