In vitro and in vivo electron transfer to the triheme cytochrome subunit bound to the photosynthetic reaction center complex in the purple bacterium Rhodovulum sulfidophilum.
In vitro and in vivo electron transfer to the triheme cytochrome subunit bound to the photosynthetic reaction center complex in the purple bacterium Rhodovulum sulfidophilum.
复制标题
体外和体内电子转移到与紫色细菌嗜硫红酵母中光合反应中心复合体结合的三血红素细胞色素亚基。
DOI:
10.1016/s0005-2728(01)00177-3
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发表时间:
2001
期刊:
影响因子:
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通讯作者:
K. Matsuura
中科院分区:
文献类型:
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作者:
M. Yoshida;S. Masuda;K. Nagashima;A. Verméglio;K. Shimada;K. Matsuura
The cytochrome subunit bound to the photosynthetic reaction center (RC) complex in Rhodovulum sulfidophilum lacks one heme-binding motif (CXXCH) out of four motifs found in other purple bacteria resulting in the absence of the most distal heme from the RC-core complex (S. Masuda et al., J. Biol. Chem. 274 (1999) 10795). Cytochrome c2, which acts as the electron donor to the RC was purified, and its gene was cloned and sequenced. The redox midpoint potential of cytochrome c2was determined to be Em=357 mV. The photo-oxidation and re-reduction of purified cytochrome c2were observed in the presence of membrane preparations. Flash-induced photo-oxidation and re-reduction of the RC-bound cytochrome were also observed in intact cells. Despite the unusual nature of the RC-bound cytochrome subunit, the cyclic electron transfer system in Rdv. sulfidophilum was shown to be similar to those in other purple bacteria.
DOI:
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发表时间:
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