Isolation and characterization of soluble electron transfer proteins from Chromatium purpuratum.
Isolation and characterization of soluble electron transfer proteins from Chromatium purpuratum.
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从 Chromatium purpuratum 中分离和表征可溶性电子转移蛋白。
DOI:
10.1021/bi952731v
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发表时间:
1996
期刊:
影响因子:
--
通讯作者:
Knaff,DB
中科院分区:
文献类型:
--
作者:
Kerfeld,CA;Chan,C;Hirasawa,M;Kleis-SanFrancisco,S;Yeates,TO;Knaff,DB
Several soluble electron transfer proteins were isolated and characterized from the marine purple-sulfur bacteriumChromatiumpurpuratum. TheC. purpuratumflavocytochromecis similar in molecular mass (68 kDa) and isoelectric point (6.5) to flavocytochromes isolated from other phototrophs. Redox titrations of the flavocytochromechemes show two components with midpoint potential values of +15 and −120 mV, behavior similar to that observed with the flavocytochrome isolated from the thermophilicChromatium tepidum.Moreover, N-terminal amino acid sequence analysis of both the flavin and the cytochrome subunit indicates substantial homology to the primary structure of the flavocytochromecofChromatium vinosum. In contrast, theC. purpuratumhigh-potential iron−sulfur protein (HiPIP) differs from those isolated from other photosynthetic bacteria in its relatively high midpoint potential (+390 mV) and the possibility that it exists as a dimer in solution. Two low molecular massc-type cytochromes were also characterized. One appears to be a high-potential (+310 mV)c8-type cytochrome. Amino acid sequencing suggests that the second cytochrome may be a homologue of the low-potential cytochromec-551, previously described in two species of Ectothiorhodospirillaceae.