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- W1998315122 abstract "Abstract The dynamic complex formed between two redox proteins, cytochrome c peroxidase (ccp) and cytochrome c (cytc), was characterized by energy transfer measurements. In Mgccp, magnesium porphyrin is substituted for heme to produce a fluorescent ccp donor; the heme in cytc acts as an energy acceptor. At low temperatures (77 K) Mgccp shows a simple decay when alone in solution but exhibits a complex behavior when bound to cytc. At room temperature the decay is simplified. This suggests a highly plastic binding domain in which conformational states of the cytc:ccp complex trapped at low temperature reequilibrate on the nanosecond time scale. The oxidation state of cytc also effects the nature of the complex. The reduced cytc shows a higher affinity for ccp and for three peroxidase mutants with surface mutations of Asp − − ≤ Lys at positions 37, 79 and 217 as demonstrated via the ionic strength dependent binding behavior of all four to a cytc affinity column. Higher affinity of CcP for reduced cytc over oxidized is consistent with the direction of electron transfer of the peroxidase reaction from the reduced to the oxidized forms of cytc and subsequent release of oxidized cytc product." @default.
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- W1998315122 date "1991-01-01" @default.
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- W1998315122 title "The Dynamics and Oxidation State Dependence of Complex Formation between Cytochrome C Peroxidase and Cytochrome C" @default.
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- W1998315122 doi "https://doi.org/10.1080/00268949108041187" @default.
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