Organization and structure of the genes for the cytochromeb/c1 complex in purple photosynthetic bacteria. A phylogenetic study describing the homology of theb/c1 subunits between prokaryotes, mitochondria, and chloroplasts
Organization and structure of the genes for the cytochromeb/c1 complex in purple photosynthetic bacteria. A phylogenetic study describing the homology of theb/c1 subunits between prokaryotes, mitochondria, and chloroplasts
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紫色光合细菌细胞色素b/c1复合物基因的组织和结构。
DOI：
--
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发表时间：
1988
影响因子：
3
通讯作者：
N. Gabellini
中科院分区：
文献类型：
--
作者：
N. Gabellini
细胞色素b/c1复合物是一种普遍存在的能量转导酶，是原核生物、线粒体和叶绿体（b6/f）电子传递链的一部分。在古老的紫色光合细菌中，b/c1复合体占据着代谢的中心角色，是光合和呼吸电子传递链的一部分。在红细菌中，b/c1复合物的三个亚基是FeS蛋白、细胞色素b和细胞色素1，它们由一个组成型表达的操纵子fbc编码。将描述细胞色素b/c1复合物的基因的组织、转录方式和编码多肽的生物发生。用于分离fbc基因的Rhodobacter，以前报道为R. sphaeroides为R.囊状的对原核生物b/c1复合物的进一步生化特性分析表明，fbc操纵子编码的3个多肽包含了完整的催化结构：泛喹啉-细胞色素-c还原酶。这三种氧化还原多肽的序列高度同源。capsulatus和酵母线粒体（细胞色素b 41%，FeS蛋白46%，细胞色素1 31%）提供了线粒体起源于紫色细菌系统发育线的进一步证据。细胞色素b的结构也表现出相当大的同源性叶绿体细胞色素b 6+亚基IV（26%）。从R.而叶绿体只有C-末端部分是保守的（14%的总同源性），而细胞色素1和细胞色素f之间的同源性很弱（12%），尽管这两种多肽的拓扑结构相似。同源性分析表明，催化位点醌醇氧化酶（Qo）和醌还原酶（Qi）是同源的，而细胞色素和质体蓝素还原酶位点不是同源的，可能通过趋同进化来自不同的祖先基因。
The cytochromeb/c1 complex is an ubiquitous energy transducing enzyme, part of the electron transport chain of prokaryotes, mitochondria, and chloroplasts (b6/f). In the ancient purple photosynthetic bacteria, theb/c1 complex occupies a central metabolic role, being part of their photosynthetic and respiratory electron transport chain. InRhodobacter the three subunits of theb/c1 complex are FeS protein, cytochromeb, and cytochromec1, and they are encoded by a constitutively expressed operon namedfbc. The organization of the genes for the cytochromeb/c1 complex, the modality of transcription, and the biogenesis of the encoded polypeptides will be described. TheRhodobacter species used to isolate thefbc genes, previously reported asR. sphaeroides was identified asR. capsulatus. Further biochemical characterization of the prokaryoticb/c1 complex indicated that the three polypeptides encoded by thefbc operon comprise the entire catalytic structure: ubiquinol-cytochrome-c reductase.The amino acid sequences of the threeb/c1 subunits from the photosynthetic bacteriumRhodobacter capsulatus were compared with the corresponding sequences from yeast mitochondria and spinach chloroplasts. The high homology found between the sequences of all three redox polypeptides fromR. capsulatus and yeast mitochondria (cytochromeb 41%, FeS protein 46%, cytochromec1 31%) provided further evidence that mitochondria arose from the phylogenetic line of purple bacteria. The structure of cytochromeb also exhibited considerable homology to chloroplast cytochromeb6 plus subunit IV (26%). The amino acid sequence of the Rieske FeS protein fromR. capsulatus and chloroplasts were found to be conserved only in the C-terminal part (14% total identity), whereas the homology between cytochromec1 and cytochromef is very weak (12%), despite similar topology of the two polypeptides.Analysis of the homology suggested that the catalytic sites quinol oxidase (Qo) and quinone reductase (Qi) arose monophonetically, whereas cytochromec and plastocyanin reductase sites are not homologous and could derive from diverse ancestral genes by convergent evolution.
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fbc 操纵子，编码先前从球形红假单胞菌中描述的 Rieske Fe-S 蛋白细胞色素 b 和细胞色素 c1 脱辅基蛋白，来自荚膜红假单胞菌。
影响因子：
5.6
作者：
Davidson,E;Daldal,F
通讯作者：
Daldal,F
牛心细胞色素 c1 制剂中不含血红素的蛋白质与介导 c1-c 复合物形成的蛋白质（一种高谷氨酸含量的蛋白质）的同一性。
影响因子：
2.7
作者：
Wakabayashi,S;Takeda,H;Matsubara,H;Kim,CH;King,TE
通讯作者：
King,TE
嗜热栖热菌 Rieske 铁硫蛋白的纯化和表征。
DOI：
--
发表时间：
1984
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Fee,JA;Findling,KL;Yoshida,T;Hille,R;Tarr,GE;Hearshen,DO;Dunham,WR;Day,EP;Kent,TA;Münck,E
通讯作者：
Münck,E
DOI：
--
发表时间：
1980
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Nobrega,FG;Tzagoloff,A
通讯作者：
Tzagoloff,A
DOI：
10.1016/s0021-9258(18)47500-x
发表时间：
1987-06
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
J. Beckmann;P. Ljungdahl;J. L. Lopez;B. Trumpower
通讯作者：
J. Beckmann;P. Ljungdahl;J. L. Lopez;B. Trumpower