Abstract
Au-protein from Micrococcus luteus, with and without Au inactive center, and chloroauric acid (HAu IIICl4·4H2O) with the addition of rutin, catechol, and riboflavin have been studied by means of electrochemistry and ESR. The redox potentials for Au-protein, as well as for the complexes Au-rutin and Au-catechol, have been measured, and ESR spectra of complexes Au-rutin and Au-catechol have been recorded. It has been shown that the Au atom binds to Au-protein via OH-groups of rutin. Flavin does not participatein gold binding. Au-protein is characterized by two peaks of cyclic voltammogram, −0.37 and −0.54 V. Au-protein with these potentials is able to function in the electron-transport chain of membranes between flavoproteins and quinones.
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Levchenko, L.A., Kulakovskaya, S.I., Kulikov, A.V. et al. Electrochemical and ESR studies of au-protein from Micrococcus luteus . Appl Biochem Biotechnol 88, 201–210 (2000). https://doi.org/10.1385/ABAB:88:1-3:201
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DOI: https://doi.org/10.1385/ABAB:88:1-3:201