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Rational redox tuning of transition metal sites: Learning from superoxide reductase

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JournalChemical Communications
DateAccepted/In press - 8 Jul 2019
DateE-pub ahead of print (current) - 8 Jul 2019
Issue number62
Volume55
Number of pages4
Pages (from-to)9148-9151
Early online date8/07/19
Original languageEnglish

Abstract

Using superoxide reductase as a model system, a computational approach reveals how histidine tautomerism tunes the redox properties of metalloenzymes to enable their catalytic function. Inspired by these experimentally inaccessible insights, non-canonical histidine congeners are introduced as new versatile tools for the rational engineering of biological transition metal sites.

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