2mi7 | pdb_00002mi7

Solution NMR structure of alpha3Y

spinqualitylabelsall models 2mi7, 32 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mi7 is a 1 chain structure with sequence from Synthetic construct sequences. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1lq7, 2lxy Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Tyrosine oxidation-reduction involves proton-coupled electron transfer (PCET) and a reactive radical state. These properties are effectively controlled in enzymes that use tyrosine as a high-potential, one-electron redox cofactor. The alpha3Y model protein contains Y32, which can be reversibly oxidized and reduced in voltammetry measurements. Structural and kinetic properties of alpha3Y are presented. A solution NMR structural analysis reveals that Y32 is the most deeply buried residue in alpha3Y. Time-resolved spectroscopy using a soluble flash-quench generated [Ru(2,2'-bipyridine)3]3+ oxidant provides high-quality Y32-O* absorption spectra. The rate constant of Y32 oxidation (kPCET) is pH dependent: 1.4 x 104 M-1 s-1 (pH 5.5), 1.8 x 105 M-1 s-1 (pH 8.5), 5.4 x 103 M-1 s-1 (pD 5.5), and 4.0 x 104 M-1 s-1 (pD 8.5). kH/kD of Y32 oxidation is 2.5 +/- 0.5 and 4.5 +/- 0.9 at pH(D) 5.5 and 8.5, respectively. These pH and isotope characteristics suggest a concerted or stepwise, proton-first Y32 oxidation mechanism. The photochemical yield of Y32-O* is 28-58% versus the concentration of [Ru(2,2'-bipyridine)3]3+. Y32-O* decays slowly, t1/2 in the range of 2-10 s, at both pH 5.5 and 8.5, via radical-radical dimerization as shown by second-order kinetics and fluorescence data. The high stability of Y32-O* is discussed relative to the structural properties of the Y32 site. Finally, the static alpha3Y NMR structure cannot explain (i) how the phenolic proton released upon oxidation is removed or (ii) how two Y32-O* come together to form dityrosine. These observations suggest that the dynamic properties of the protein ensemble may play an essential role in controlling the PCET and radical decay characteristics of alpha3Y. Photochemical Tyrosine Oxidation in the Structurally Well-Defined alphaY Protein: Proton-Coupled Electron Transfer and a Long-Lived Tyrosine Radical.,Glover SD, Jorge C, Liang L, Valentine KG, Hammarstrom L, Tommos C J Am Chem Soc. 2014 Aug 14. PMID:25121576 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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