Silvia H Libardi, Helene Pindstrup, Daniel R Cardoso, Leif H Skibsted
The hypervalent meat pigment ferrylmyoglobin, MbFe(IV)═O, characteristic for oxidatively stressed meat and known to initiate protein cross-linking, was found to be reduced by hydrogen sulfide to yield sulfmyoglobin. Horse heart myoglobin, void of cysteine, was used to avoid possible interference from protein thiols. For aqueous solution, the reactions were found to be second-order, and an apparent acid catalysis could be quantitatively accounted for in terms of a fast reaction between protonated ferrylmyoglobin, MbFe(IV)═O,H(+), and hydrogen sulfide, H2S (k2 = (2...
March 20, 2013: Journal of Agricultural and Food Chemistry