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Distinguishing Protonation States of Histidine Ligands to the Oxidized Rieske Iron–Sulfur Cluster through 15N Vibrational Frequency Shifts
Authors:Benjamin R. Jagger  Ashlyn M. Koval  Prof. Ralph A. Wheeler
Affiliation:Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA, USA
Abstract:
The Rieske [2Fe–2S] cluster is a vital component of many oxidoreductases, including mitochondrial cytochrome bc1; its chloroplast equivalent, cytochrome b6f; one class of dioxygenases; and arsenite oxidase. The Rieske cluster acts as an electron shuttle and its reduction is believed to couple with protonation of one of the cluster′s His ligands. In cytochromes bc1 and b6f, for example, the Rieske cluster acts as the first electron acceptor in a modified Q cycle. The protonation states of the cluster′s His ligands determine its ability to accept a proton and possibly an electron through a hydrogen bond to the electron carrier, ubiquinol. Experimental determination of the protonation states of a Rieske cluster′s two His ligands by NMR spectroscopy is difficult, due to the close proximity of the two paramagnetic iron atoms of the cluster. Therefore, this work reports density functional calculations and proposes that difference vibrational spectroscopy with 15N isotopic substitution may be used to assign the protonation states of the His ligands of the oxidized Rieske [2Fe–2S] complex.
Keywords:broken symmetry  cytochromes  density functional calculations  electron transfer  Rieske
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