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Kerfeld, C. A. , Chan, C. and Yeates, T. O. : Biochemical Characterization and Three-Dimensional Structure of Dimeric High Potential Iron-sulfur Protein from Chromatium purpuratum. Photosynthesis: From Light to Biosphere 2: 757-760. 1995.
High-potential iron-sulfur proteins (HiPIPs) form a unique family of Fe4S4 ferredoxins that function in anaerobic electron transport chains. Some HiPIPs have a redox potential higher than any other known iron-sulfur protein (e. g. , HiPIP from Rhodopila globiformis has a redox potential of ca. 450 mV). Several HiPIPs have so far been characterized structurally, their folds belonging to the a+ß class.
ferrooxidans include: sqr (AFE_1792) encoding sulfide quinone reductase from NASF-1 strain [26,52], doxDA (AFE_0044) encoding thiosulfate quinone oxidoreductase from ATCC23270  and from the CCM4253 strain , tetH (AFE_0029) encoding tetrathionate hydrolase from ATCC23270 , cydAB (AFE_0955-0954) encoding a bd oxidase and cyoABCD (AFE_0631-0634) encoding a bo3 oxidase from ATCC19859  (See Figure 2). All these genes are upregulated in sulfur-containing media relatively to Fe(II) (Table 2[24-29] and Table 3[7,24-26,28,29]). This is also the case for the petII operon (AFE_2727-2732) encoding a second bc1 complex, a cytochrome c4, SdrA2 and a high potential iron-sulfur protein.
Reaction Center and High-Potential Iron-Sulfur Protein.