Quercetin as an inhibitor of hemoglobin-mediated lipid oxidation: Mechanisms of action and use of molecular docking

Haizhou Wu; Jie Yin; Shulan Xiao; Jianhao Zhang; Mark P Richards

doi:10.1016/j.foodchem.2022.132473

Quercetin as an inhibitor of hemoglobin-mediated lipid oxidation: Mechanisms of action and use of molecular docking

Food Chem. 2022 Aug 1:384:132473. doi: 10.1016/j.foodchem.2022.132473. Epub 2022 Feb 17.

Authors

Haizhou Wu¹, Jie Yin², Shulan Xiao³, Jianhao Zhang⁴, Mark P Richards⁵

Affiliations

¹ National Center of Meat Quality, Safety Control, Jiangsu Innovation Center of Meat Production, Processing, College of Food Science, Technology, Nanjing Agricultural University, Nanjing 210095, PR China; Department of Animal and Dairy Sciences, University of Wisconsin-Madison, Meat Science and Animal Biologics Discovery Program, 1933 Observatory Dr. Madison, WI 53706, United States; Department of Biology and Biological Engineering-Food and Nutrition Science, Chalmers University of Technology, SE 412 96 Gothenburg, Sweden.
² Department of Animal and Dairy Sciences, University of Wisconsin-Madison, Meat Science and Animal Biologics Discovery Program, 1933 Observatory Dr. Madison, WI 53706, United States.
³ National Center of Meat Quality, Safety Control, Jiangsu Innovation Center of Meat Production, Processing, College of Food Science, Technology, Nanjing Agricultural University, Nanjing 210095, PR China.
⁴ National Center of Meat Quality, Safety Control, Jiangsu Innovation Center of Meat Production, Processing, College of Food Science, Technology, Nanjing Agricultural University, Nanjing 210095, PR China. Electronic address: jianhao_zhang@163.com.
⁵ Department of Animal and Dairy Sciences, University of Wisconsin-Madison, Meat Science and Animal Biologics Discovery Program, 1933 Observatory Dr. Madison, WI 53706, United States. Electronic address: mprichards@wisc.edu.

PMID: 35219235
DOI: 10.1016/j.foodchem.2022.132473

Abstract

The antioxidant effect of quercetin on hemoglobin(Hb)-mediated lipid oxidation and the mechanisms involved were investigated. Quercetin strongly inhibited Hb-mediated lipid oxidation in washed muscle. Quercetin showed effective hydroxyl radical scavenging ability similar to butylated hydroxytoluene (BHT). Quercetin reduced metHb resulting in formation of oxyHb. Bound quercetin decreased heme dissociation from metHb. Conversion to oxyHb and decreased heme dissociation represent routes to limit Hb-mediated lipid oxidation. Electrospray ionization mass spectrometry (ESI-MS) indicated one molecule of quercetin was covalently bound to Hb α-chain. Quercetin quinone docked 3.3 Å from the thiol of αCys(H15) but not near any other Cys residues of turkey Hb. At the docking site, hydrogen bonding between quercetin quinone and amino acids of α- and β-chain was demonstrated. This represents a path by which quercetin became covalently bound to α-chain. Molecular docking of heme proteins to polyphenols provides a template to better understand antioxidant interactions in muscle foods.

Keywords: Antioxidant; Covalently bound; Flavonoids; Heme protein; Hemin loss; Meat; Structural change.

MeSH terms

Antioxidants / chemistry
Heme / chemistry
Hemoglobins* / antagonists & inhibitors
Hemoglobins* / chemistry
Hemoglobins* / metabolism
Lipids* / chemistry
Molecular Docking Simulation
Oxidation-Reduction / drug effects
Quercetin* / chemistry
Quercetin* / pharmacology

Substances

Antioxidants
Hemoglobins
Lipids
Heme
Quercetin