Ferryl (Fe(IV)=O) species are involved in key enzymatic processes with direct biomedical relevance; among others, the uncontrolled reactivities of ferryl Mb (myoglobin) and Hb (haemoglobin) have been reported to be central to the pathology of rhabdomyolysis and subarachnoid haemorrhage. Rapid-scan stopped-flow methods have been used to monitor the spectra of the ferryl species in Mb and Hb as a function of pH. The ferryl forms of both proteins display an optical transition with pK∼4.7, and this is assigned to protonation of the ferryl species itself. We also demonstrate for the first time a direct correlation between Hb/Mb ferryl reactivity and ferryl protonation status, simultaneously informing on chemical mechanism and toxicity and with broader biochemical implications.
Ferryl haem protonation gates peroxidatic reactivity in globins
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Radu Silaghi-Dumitrescu, Brandon J. Reeder, Peter Nicholls, Chris E. Cooper, Michael T. Wilson; Ferryl haem protonation gates peroxidatic reactivity in globins. Biochem J 1 May 2007; 403 (3): 391–395. doi: https://doi.org/10.1042/BJ20061421
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