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• W2015930275 abstract "Single-Cu-containing galactose oxidase in the GOasesemi state (CuII, no Tyr• radical) reacts with pulse radiolysis generated formate radicals CO2•- to give an intermediate UV−vis spectrum assigned as RSSR•-, peak at 450 nm (ε = 8100 M-1 cm-1). From a detailed kinetic analysis at 450 nm, pH 7.0, the following steps have been identified. First the strongly reducing CO2•- (−1.9V) reduces GOasesemi (k0 ≥ 6.5 × 108 M-1 s-1) to a species GOasesemi•-. This is followed by biphasic reactions (i) GOasesemi•- + GOasesemi (k1 = 1.6 × 107 M-1 s-1) to give GOasesemi + P•- and (ii) P•- + GOasesemi (k2 = 6.7 × 106 M-1 s-1) to give GOasesemiRSSR•-. There are no significant absorbance changes for the formation of GOasesemi•- and P•-, which are CuI (or related) species. However, GOasesemiRSSR•- has an absorption spectrum which differs significantly from that of GOasesemi. The 450 nm peak is characteristic of an RSSR•- radical with two cysteines in close sequence proximity and is here assigned to Cys515−Cys518, which is at the GOase surface and 10.2 Å from the Cu. On chemical modification of the RSSR group with HSPO32- to give RSSPO3H- and RS-, absorbance changes are ∼50% of those previously observed. The decay of RSSR•- (0.17 s-1) results in the formation of GOasered. No RSSR•- formation is observed in the reaction of GOasesemi Tyr495Phe with CO2•-, and a single process giving GOaseredTyr495Phe occurs. Similarly in the reaction of GOaseox with CO2•-, a single-stage reaction gives GOasesemi." @default.
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• W2015930275 date "2002-03-13" @default.
• W2015930275 modified "2023-10-11" @default.
• W2015930275 title "Pulse Radiolysis Studies on Galactose Oxidase" @default.
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• W2015930275 doi "https://doi.org/10.1021/ic0109344" @default.
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