Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein

被引:159
作者
Carrell, CJ [1 ]
Zhang, HM [1 ]
Cramer, WA [1 ]
Smith, JL [1 ]
机构
[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
关键词
cytochrome b(6)f complex; cytochrome f; energy transduction; plastoquinone; proton translocation;
D O I
10.1016/S0969-2126(97)00309-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Background: The cytochrome b(6)f complex functions in oxygenic photosynthesis as an integral membrane protein complex that mediates coupled electron transfer and proton translocation. The Rieske [2Fe-2S] protein subunit of the complex functions at the electropositive (p) membrane interface as the electron acceptor for plastoquinol and donor for the cytochrome f subunit, and may have a dynamic role in catalyzing electron and proton transfer at the membrane interface, There are significant structure/function similarities to the cytochrome bc(1) complex of the respiratory chain. Results: The 1.83 Angstrom crystal structure of a 139-residue C-terminal fragment of the Rieske [2Fe-2S] protein, derived from the cytochrome b(6)f complex of spinach chloroplasts, has been solved by multiwavelength anomalous diffraction. The structure of the fragment comprises two domains: a small 'cluster-binding' subdomain and a large subdomain. The [2Fe-2S] cluster-binding subdomains of the chloroplast and mitochondrial Rieske proteins are virtually identical, whereas the large subdomains are strikingly different despite a common folding topology. A structure-based sequence alignment of the b(6)f and be, groups of Rieske soluble domains is presented. Conclusions: The segregation of structural conservation and divergence in the cluster-binding and large subdomains of the Rieske protein correlates with the overall relatedness of the cytochrome b(6)f and bc(1) complexes, in which redox domains in the aqueous p phase are dissimilar and those within the membrane are similar. Distinct sequences and surface charge distributions among Rieske large subdomains may provide a signature for interaction with the p-side oxidant protein and for the pH of the intraorganelle compartment.
引用
收藏
页码:1613 / 1625
页数:13
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