Determination of the Proton Environment of High Stability Menasemiquinone Intermediate in Escherichia coli Nitrate Reductase A by Pulsed EPR - Archive ouverte HAL Access content directly
Journal Articles Journal of Biological Chemistry Year : 2012

Determination of the Proton Environment of High Stability Menasemiquinone Intermediate in Escherichia coli Nitrate Reductase A by Pulsed EPR

Abstract

Background: Escherichia coli nitrate reductase A highly stabilizes a semiquinone catalytic intermediate. Results: Three proton hyperfine couplings to this radical with atypical characteristics are characterized. Conclusion: Semiquinone binding is strongly asymmetric and occurs via a single short in-plane H-bond. Significance: Learning how the protein environment tunes the semiquinone properties is crucial for understanding the quinol utilization mechanism by energy-transducing enzymes.
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hal-03248799 , version 1 (03-06-2021)

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Stéphane Grimaldi, Rodrigo Arias‐cartin, Pascal Lanciano, Sevdalina Lyubenova, Rodolphe Szenes, et al.. Determination of the Proton Environment of High Stability Menasemiquinone Intermediate in Escherichia coli Nitrate Reductase A by Pulsed EPR. Journal of Biological Chemistry, 2012, 287 (7), pp.4662-4670. ⟨10.1074/jbc.M111.325100⟩. ⟨hal-03248799⟩

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