An isolated reaction center complex from the green sulfur bacterium Chlorobium vibrioforme can photoreduce ferredoxin at high rates
An isolated reaction center complex from the green sulfur bacterium Chlorobium vibrioforme can photoreduce ferredoxin at high rates
复制标题
来自绿色硫细菌 Chlorobium vibrioforme 的分离反应中心复合物可以高速率光还原铁氧还蛋白
作者：
B. Kjær;H. Scheller
以绿硫菌弧菌为原料，在厌氧条件下制备了无叶绿体膜和具有明确亚基组成的反应中心配合物。该反应中心复合物含有一个15 kda的多肽，其n端氨基酸序列为MEPQLSRPETASNQVR/。该序列与绿藻（Chlorobium limicola） pscD基因产物的n端几乎相同（Hager-Braun et al. (1995) Biochemistry 34: 9617-9624）。在铁氧化还蛋白和铁氧化还蛋白：NADP+氧化还原酶存在的情况下，膜和分离的反应中心复合物分别以333和110 μmol (mg细菌叶绿素a)−1 h−1的速率光还原NADP+。这表明孤立的反应中心配合物包含了稳态电子传递所必需的所有组分。用氧化还原滴定法测定pH 7.0时细胞色素c551的中点电位为160 mV， P840的中点电位为245 mV。抗细胞色素c551的抗体抑制NADP+的还原，而抗细菌叶绿素a结合的Fenna-Matthews-Olson蛋白的抗体则无此作用。
Chlorosome-depleted membranes and a reaction center complex with well-defined subunit composition were prepared from the green sulfur bacterium Chlorobium vibrioforme under anaerobic conditions. The reaction center complex contains a 15-kDa polypeptide with the N-terminal amino acid sequence MEPQLSRPETASNQVR/. This sequence is nearly identical to the N-terminus of the pscD gene product from Chlorobium limicola (Hager-Braun et al. (1995) Biochemistry 34: 9617–9624). In the presence of ferredoxin and ferredoxin:NADP+ oxidoreductase, the membranes and the isolated reaction center complex photoreduced NADP+ at rates of 333 and 110 μmol (mg bacteriochlorophyll a)−1 h−1, respectively. This shows that the isolated reaction center complex contains all the components essential for steady state electron transport. Midpoint potentials at pH 7.0 of 160 mV for cytochrome c551 and of 245 mV for P840 were determined by redox titration. Antibodies against cytochrome c551 inhibit NADP+ reduction while antibodies against the bacteriochlorophyll a-binding Fenna-Matthews-Olson protein do not.
影响因子：
2.9
作者：
FLING, SP;GREGERSON, DS
通讯作者：
GREGERSON, DS
光养绿硫细菌细胞色素 c-555 的纯化和性质。
影响因子：
--
作者：
Meyer,TE
通讯作者：
Meyer,TE