TY - JOUR
T1 - A new membrane-bound b-type cytochrome, cytochrome b-558, from photosynthetically grown Rhodopseudomonas sphaeroides
AU - Iba, Koh
AU - Takamiya, Ken Ichiro
N1 - Funding Information:
We are grateful to Professor M. Nishimura for his valuable discussionsa nd suggestions,a nd encouragement during this study. We also thank Professor S. Iwanaga for his help in the amino acid analysis. Part of this study was financially supportedb y grants from the Japanese Ministry of Education, Sciencea nd Culture (59480010a)n d from the Mitsubishi Foundation.
PY - 1986/4
Y1 - 1986/4
N2 - A new membrane-bound b-type cytochrome, cytochrome b-558, was removed from chromatophore membranes of photosynthetically grown Rhodopseudomonas sphaeroides strain R-26 by deoxycholate-cholate extraction. The cytochrome was purified by ammonium sulfate fractionation and ion-exchange chromatography. Cytochrome b-558 had absorption maxima at 280 and 405 nm in the oxidized form, and at 558, 528, and 420 nm in the reduced form. It had a midpoint potential of -130 mV at pH 7.0. The minimal molecular weight of this protein was 42,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and it contained one mole heme per mole of protein. The isoelectric point was 8.5. The electrophoretic pattern of heme-carrying proteins and the redox potentiometry showed that cytochrome b-558 was present in membranes from wild type, strain R-26, and strain GA grown photosynthetically, but not from any strain grown aerobically.
AB - A new membrane-bound b-type cytochrome, cytochrome b-558, was removed from chromatophore membranes of photosynthetically grown Rhodopseudomonas sphaeroides strain R-26 by deoxycholate-cholate extraction. The cytochrome was purified by ammonium sulfate fractionation and ion-exchange chromatography. Cytochrome b-558 had absorption maxima at 280 and 405 nm in the oxidized form, and at 558, 528, and 420 nm in the reduced form. It had a midpoint potential of -130 mV at pH 7.0. The minimal molecular weight of this protein was 42,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and it contained one mole heme per mole of protein. The isoelectric point was 8.5. The electrophoretic pattern of heme-carrying proteins and the redox potentiometry showed that cytochrome b-558 was present in membranes from wild type, strain R-26, and strain GA grown photosynthetically, but not from any strain grown aerobically.
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U2 - 10.1016/0003-9861(86)90484-4
DO - 10.1016/0003-9861(86)90484-4
M3 - Article
C2 - 3485957
AN - SCOPUS:0022546029
VL - 246
SP - 391
EP - 395
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -