Riboflavin photosensitized oxidation of myoglobin

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Riboflavin photosensitized oxidation of myoglobin. / Grippa, Juliana M.; Zawadzki, Andressa; Grossi, Alberto Blak; Skibsted, Leif Horsfelt; Cardoso, Daniel R.

In: Journal of Agricultural and Food Chemistry, Vol. 62, No. 5, 2014, p. 1153-1158.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Grippa, JM, Zawadzki, A, Grossi, AB, Skibsted, LH & Cardoso, DR 2014, 'Riboflavin photosensitized oxidation of myoglobin', Journal of Agricultural and Food Chemistry, vol. 62, no. 5, pp. 1153-1158. https://doi.org/10.1021/jf405182f

APA

Grippa, J. M., Zawadzki, A., Grossi, A. B., Skibsted, L. H., & Cardoso, D. R. (2014). Riboflavin photosensitized oxidation of myoglobin. Journal of Agricultural and Food Chemistry, 62(5), 1153-1158. https://doi.org/10.1021/jf405182f

Vancouver

Grippa JM, Zawadzki A, Grossi AB, Skibsted LH, Cardoso DR. Riboflavin photosensitized oxidation of myoglobin. Journal of Agricultural and Food Chemistry. 2014;62(5):1153-1158. https://doi.org/10.1021/jf405182f

Author

Grippa, Juliana M. ; Zawadzki, Andressa ; Grossi, Alberto Blak ; Skibsted, Leif Horsfelt ; Cardoso, Daniel R. / Riboflavin photosensitized oxidation of myoglobin. In: Journal of Agricultural and Food Chemistry. 2014 ; Vol. 62, No. 5. pp. 1153-1158.

Bibtex

@article{bf93ba3fcb8141f2ae3524c005e89e3d,
title = "Riboflavin photosensitized oxidation of myoglobin",
abstract = "The reaction of the fresh meat pigment oxymyoglobin, MbFe(II)O, and its oxidized form metmyoglobin, MbFe(III), with triplet-state riboflavin involves the pigment protein, which is oxidatively cleaved or dimerized as shown by SDS-PAGE and Western blotting. The overall rate constant for oxidation of MbFe(II)O by Rib is (3.0 ± 0.5) × 10 L·mol·s and (3.1 ± 0.4) × 10 L·mol·s for MbFe(III) in phosphate buffer of pH 7.4 at 25 C as determined by laser flash photolysis. The high rates are rationalized by ground state hydrophobic interactions as detected as static quenching of fluorescence from singlet-excited state riboflavin by myoglobins using time-resolved fluorescence spectroscopy and a Stern-Volmer approach. Binding of riboflavin to MbFe(III) has K = (1.2 ± 0.2) × 10 mol·L with ΔH = -112 ± 22 kJ·mol and ΔS = -296 ± 75 J·mol·K. For meat, riboflavin is concluded to be a photosensitizer for protein oxidation but not for discoloration.",
author = "Grippa, {Juliana M.} and Andressa Zawadzki and Grossi, {Alberto Blak} and Skibsted, {Leif Horsfelt} and Cardoso, {Daniel R.}",
year = "2014",
doi = "10.1021/jf405182f",
language = "English",
volume = "62",
pages = "1153--1158",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "5",

}

RIS

TY - JOUR

T1 - Riboflavin photosensitized oxidation of myoglobin

AU - Grippa, Juliana M.

AU - Zawadzki, Andressa

AU - Grossi, Alberto Blak

AU - Skibsted, Leif Horsfelt

AU - Cardoso, Daniel R.

PY - 2014

Y1 - 2014

N2 - The reaction of the fresh meat pigment oxymyoglobin, MbFe(II)O, and its oxidized form metmyoglobin, MbFe(III), with triplet-state riboflavin involves the pigment protein, which is oxidatively cleaved or dimerized as shown by SDS-PAGE and Western blotting. The overall rate constant for oxidation of MbFe(II)O by Rib is (3.0 ± 0.5) × 10 L·mol·s and (3.1 ± 0.4) × 10 L·mol·s for MbFe(III) in phosphate buffer of pH 7.4 at 25 C as determined by laser flash photolysis. The high rates are rationalized by ground state hydrophobic interactions as detected as static quenching of fluorescence from singlet-excited state riboflavin by myoglobins using time-resolved fluorescence spectroscopy and a Stern-Volmer approach. Binding of riboflavin to MbFe(III) has K = (1.2 ± 0.2) × 10 mol·L with ΔH = -112 ± 22 kJ·mol and ΔS = -296 ± 75 J·mol·K. For meat, riboflavin is concluded to be a photosensitizer for protein oxidation but not for discoloration.

AB - The reaction of the fresh meat pigment oxymyoglobin, MbFe(II)O, and its oxidized form metmyoglobin, MbFe(III), with triplet-state riboflavin involves the pigment protein, which is oxidatively cleaved or dimerized as shown by SDS-PAGE and Western blotting. The overall rate constant for oxidation of MbFe(II)O by Rib is (3.0 ± 0.5) × 10 L·mol·s and (3.1 ± 0.4) × 10 L·mol·s for MbFe(III) in phosphate buffer of pH 7.4 at 25 C as determined by laser flash photolysis. The high rates are rationalized by ground state hydrophobic interactions as detected as static quenching of fluorescence from singlet-excited state riboflavin by myoglobins using time-resolved fluorescence spectroscopy and a Stern-Volmer approach. Binding of riboflavin to MbFe(III) has K = (1.2 ± 0.2) × 10 mol·L with ΔH = -112 ± 22 kJ·mol and ΔS = -296 ± 75 J·mol·K. For meat, riboflavin is concluded to be a photosensitizer for protein oxidation but not for discoloration.

U2 - 10.1021/jf405182f

DO - 10.1021/jf405182f

M3 - Journal article

AN - SCOPUS:84893653681

VL - 62

SP - 1153

EP - 1158

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 5

ER -

ID: 101952355