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• W2047079806 abstract "Cross-reaction rate constants k12 (22 °C) at pH 7.0 have been determined for the reduction of FeIII2 and tyrosyl-radical-containing active-R2 from E. coli ribonucleotide reductase with eight organic radicals (OR), e.g., MV•+ from methyl viologen. The more reactive OR's were generated in situ using pulse radiolysis (PR) techniques, and other OR's were generated by prior reduction of the parent with dithionite, followed by stopped-flow (SF) studies. In both procedures it was necessary to include consideration of doubly-reduced parent forms. Values of k12 are in the range 109 to 104 M-1 s-1 and reduction potentials Eo1 for the OR vary from −0.446 to +0.194 V. Samples of E. coli active-R2 also have an FeIII2 met-R2 component (with no Tyr•), which in the present work was close to 40%. From separate experiments met-R2 gave similar k12 rate constants (on average 66% bigger) to those for active-R2, suggesting that reduction of the FeIII2 center is the common rate-limiting step. A single Marcus free-energy plot of log k12 − 0.5 log f vs −Eo1/0.059 describes all the data, and the slope of 0.54 is in satisfactory agreement with the theoretical value of 0.50. It is concluded that the rate-limiting step involves electron transfer. In addition, the intercept at −Eo1/0.059 = 0 is 5.94, where values of the reduction potential and self-exchange rate constant for met-R2 contribute to this value. To maintain electroneutrality at the ∼10 Å buried active site H+ uptake is also required. For both e- and H+ transfer the conserved pathway Trp-48, Asp-237, His-118 to FeA is a possible candidate requiring further examination." @default.
• W2047079806 created "2016-06-24" @default.
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• W2047079806 date "2000-02-29" @default.
• W2047079806 modified "2023-10-16" @default.
• W2047079806 title "Mechanistic Implications of a Linear Free-Energy Correlation of Rate Constants for the Reduction of Active- and Met-R2 Forms of <i>E. coli</i> Ribonucleotide Reductase with Eight Organic Radicals" @default.
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• W2047079806 doi "https://doi.org/10.1021/ja993412k" @default.
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