Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 129, Issue 3, Pages 504-505Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja0678727
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Funding
- NIGMS NIH HHS [GM 036298, R37 GM036298, R01 GM025158, R01 GM033576, R01 GM033576-39, GM 25158, R01 GM025158-31, R01 GM036298] Funding Source: Medline
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Ultraviolet resonance Raman spectroscopy reveals that, when heated at pH 3, a substantial fraction (30%) of cytochrome c converts to a beta-sheet structure, at the expense of turns and helices. beta-sheet formation is rapid, exhibiting a 2 mu s rise time, following a temperature jump. It is proposed that a short beta-sheet segment, comprising residues 37-39 and 58-61, extends itself into the large 37-61 loop when the latter is destabilized by protonation of H26, which forms an anchoring H-bond to loop residue P44. This conformation change ruptures the Met80-Fe bond, as revealed by changes in ligation-sensitive hemeresonant Raman bands. It also induces peroxidase activity with the same temperature profile. This process is suggested to model the apoptotic peroxidation of cardiolipin by cytochrome c.
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