12rh

Structure of turkey hemoglobin A covalently bound with epigallocatechin gallate

spinqualitylabelsall models 12rh, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 12rh is a 4 chain structure with sequence from Meleagris gallopavo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.995Å Ligands: HEM, KDH, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P84479_MELGA Publication Abstract from PubMed We investigated the binding of epigallocatechin gallate (EGCG) to turkey hemoglobin A (Hb), noting that polyphenols have the capacity to inhibit oxidative deterioration in muscle foods mediated by endogenous hemoglobin. The addition of EGCG to MetHb resulted in covalently bound EGCG to Cys(130) of both alpha-chains. The crystal structure showed that each bound EGCG was located near the other and in the protein interior. Distances between the nearest phenol/phenolate of bound EGCG and the nearest iron atom of the heme moieties were 11.7-16.5 A. Antioxidative characteristics due to bound EGCG included decreases in both hemin dissociation and H(2)O(2)-mediated ferryl Hb formation, counterbalanced by increased Hb autoxidation. Bound EGCG less effectively inhibited oxyHb-mediated lipid oxidation compared to MetHb-mediated lipid oxidation. The mechanisms by which EGCG adduction affected oxidative characteristics of Hb are discussed, including electron transfer from bound EGCG to the heme, interactions with lipids, and effects of cross-linking on hemin affinity. Oxidative Characteristics of Turkey Hemoglobin A Containing Covalently Bound Epigallocatechin Gallate.,Yin J, Zhang W, Tatiyaborworntham N, Bingman CA, Richards MP J Agric Food Chem. 2026 Jun 9. doi: 10.1021/acs.jafc.5c17482. PMID:42262311 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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