1H nuclear magnetic resonance study of the protonation behaviour of the histidine residues and the electron self-exchange reaction of azurin from Alcaligenes denitrificans.
作者： C.M. Groeneveld , M.C. Ouwerling , C. Erkelens , G.W. Canters
DOI: 10.1016/0022-2836(88)90343-9
关键词:
摘要: The proton nuclear magnetic resonance spectrum of azurin from Alcaligenes denitrificans at pH 6.0 and 309 K is reported. Proton signals all methionine histidine residues (among them the copper ligands) have been assigned. data used to study behaviour His35 establish electron self-exchange rate protein. appears be protonated less than 4.5, possibly after rupture a salt bridge. No effects this protonation on tertiary structure around site are observed, however, contrary case Pseudomonas aeruginosa azurin. amounts 4 x 10(5) M-1 S-1 6.7 297 K. support conclusion that takes place by way hydrophobic surface patch His117, not involved in reaction. Oxidation increases acidity freely titrating His32 His83 0.07 0.25 pKa units, respectively. can test theory electrostatic interactions proteins. optical extinction coefficient 625 nm was experimentally determined 4.8(+/- 0.1) 10(3) cm-1.
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