Rieske-type proteins redox potential

Redox Potentials of Rieske and Rieske-Type Proteins... 

When the second-site revertants were segregated from the original mutations, the bci complexes carrying a single mutation in the linker region of the Rieske protein had steady-state activities of 70-100% of wild-type levels and cytochrome b reduction rates that were approximately half that of the wild type. In all these mutants, the redox potential of the Rieske cluster was increased by about 70 mV compared to the wild type (51). Since the mutations are in residues that are in the flexible linker, at least 27 A away from the cluster, it is extremely unlikely that any of the mutations would have a direct effect on the redox potential of the cluster that would be observed in the water-soluble fragments. However, the mutations in the flexible linker will affect the mobility of the Rieske protein. Therefore, the effect of the mutations described is due to the interaction between the positional state of the Rieske protein and its electrochemical properties (i.e., the redox potential of the cluster). 

Although the redox potential of Rieske-type clusters is approximately 400 mV lower than that of Rieske clusters, it is 300 mV more positive than the redox potential of plant-type ferredoxins (approximately -400 mV). Multiple factors have been considered to be essential for the redox potential of iron sulfur proteins ... 

Rieske protain/centar an iron-sulphur protein first isolat from Complex III of the mitochondrial electron transport chain, in which it occurs with cytochromes b and C) [J.S, Rieske el al. Biochem. Biophys Res Commun. IS (1%4) 338-344], but which has now been found in the equivalent cytochrome be complexes in the bacterial plasma membrane and the chloroplast thylakoid membrane. The latter, known as the cytochrome bff complex, partidpates in cyclic and noncyclic electron flow in the light phase of photosynthesis (see Photosynthesis). All Rieske proteins are one-electron redox systems with a standanl redox potential in the + 0.2 to + 0.3V range and have a (2Fe-2S] center, a single membrane-spanning a-helix, and a characteristic electron spin resonance (ESR) spectrum. The chloroplastidic R.p/c, with a M, of - 20,000, is smaller than that of the mitochondnon. It is encoded in the nucleus, synthesized in the cytoplasm and translocated to the chloroplast, where it is inserted into the thylakoid membrane. Within the thylakoid membrane its [2Fe-2S] redox centre (near to its C-terminus) can readily pass electrons to cytochrome /, a c-type cytochrome that projects from the luminal surface cytochrome / then passes electrons to plastocyanin (see) dissolved in the aqueous milieu of the thylakoid lumen. 

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