The primary structure of soluble cytochrome c-551 from the phototrophic green sulfur bacterium Chlorobium limicola, strain Tassajara, reveals a novel c-type cytochrome.
The primary structure of soluble cytochrome c-551 from the phototrophic green sulfur bacterium Chlorobium limicola, strain Tassajara, reveals a novel c-type cytochrome.
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来自光养绿硫细菌 Chlorobium limicola(Tassajara 菌株)的可溶性细胞色素 c-551 的一级结构揭示了一种新型 c 型细胞色素。
DOI:
10.1021/bi9806706
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发表时间:
1998
期刊:
影响因子:
--
通讯作者:
VanBeeumen,J
中科院分区:
文献类型:
--
作者:
Klarskov,K;Verte,F;VanDriessche,G;Meyer,TE;Cusanovich,MA;VanBeeumen,J
Chlorobium limicola,strain Tassajara, cytochromec-551 is a soluble dimeric protein containing identical subunits of about 30 kDa. The amino acid sequence was determined by a combination of automated Edman degradation and mass analysis. There are 258 residues with a single heme binding site located at cysteine positions 172 and 175. In addition, there is a disulfide bridge between Cys78 and Cys109, and a free cysteine at position 219 which was found to occur as cysteic acid. The only homologue of soluble cytochromec-551 is the soxA protein which is part of the thiosulfate utilization operon ofParacoccus denitrificans. They are 32% identical with three small gaps. This is consistent with the observation that cytochromec-551 is the electron acceptor for a thiosulfate-oxidizing enzyme. On the basis of the redox potential of 135 mV, the sixth heme ligand should be a methionine. Among the seven methionine residues that are present inc-551, only one is conserved, two residues ahead of the heme-binding site. The far-UV circular dichroism spectrum indicates 40% α helix and 25% β secondary structure. No other known cytochromechas such a mixed structure; they are either all helical or all β. Thus,Chlorobiumsoluble cytochromec-551 and soxA are likely to be representative of a new class ofc-type cytochromes.