Reduction of Ferrylmyoglobin by β-Lactoglobulin
- 1 January 1996
- journal article
- research article
- Published by Taylor & Francis in Free Radical Research
- Vol. 24 (6) , 429-438
- https://doi.org/10.3109/10715769609088042
Abstract
Reduction of iron (IV) in ferrylmyoglobin in the presence of P-lactoglobulin in aqueous solution is the result of two parallel reactions: (i) a so-called autoreduction, and (ii) reduction by β-lactoglobulin in a second-order-reaction resulting in bityrosine formation in β lactoglobulin. In the pH-region investigated (5.4–7.4), the rate of reduction increased for both reactions with decreasing pH. The second order-reaction had for non-denatured β-lactoglobulin the activation parameters: AH* = 45 kJ.mol-1 and AS* = -93J mol-1.K-1 at pH = 7.0 and ionic strength 0.16 (NaCl). Reduction of ferrylmyoglobin by β-lactoglobulin denatured by heat (86°C for 3 min) or by hydrostatic pressure (300 MPa for 15 min) resulted in formation of higher molecular weight species as detected by size-exclusion chromatography and by SDS-PAGE. No molecular weight changes were observed for reduction of ferrylmyoglobin by native P-lactoglobulin. Detection of bityrosine in the native β-lactoglobulin fraction after oxidation with ferrylmyoglobin indicated intra-molecular bityrosine formation. In heat-denatured β-lactoglobulin bityrosine formation could be of intra-molecular and/or of inter-molecular origin, the latter being confirmed by size- exclusion chromatography.Keywords
This publication has 30 references indexed in Scilit:
- Acid-catalysed reduction of ferrylmyoglobin: product distribution and kinetics of autoreduction and reduction by NADHZeitschrift für Lebensmittel-Untersuchung und Forschung, 1995
- The Role of H2O2-Generated Myoglobin Radical in Crosslinking of MyosinFree Radical Research, 1995
- Free radicals in inflammation: second messengers and mediators of tissue destructionBritish Medical Bulletin, 1993
- Oxidation mechanism of vitamin E analogue (Trolox C, 6-hydroxy-2,2,5,7,8-pentamethylchroman) and vitamin E by horseradish peroxidase and myoglobinArchives of Biochemistry and Biophysics, 1992
- The interaction of Trolox C, a water-soluble vitamin E analog, with ferrylmyoglobin: Reduction of the oxoferryl moietyArchives of Biochemistry and Biophysics, 1992
- Detection of an oxyferryl porphyrin .pi.-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound IBiochemistry, 1989
- Reduction of ferrylmyoglobin to metmyoglobin by quinonoid compoundsChemico-Biological Interactions, 1988
- X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymesBiochemistry, 1986
- Ultraviolet difference spectroscopy of myoglobin: assignment of pK values of tyrosyl phenolic groups and the stability of the ferryl derivativesBiochemistry, 1981
- Studies on Cytochrome c PeroxidaseJournal of Biological Chemistry, 1967