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SERR-Spectroelectrochemical Study of a cbb(3) Oxygen Reductase in a Biomimetic Construct
Citation key ISI:000261835100087
Author Todorovic, Smija and Verissimo, Andreia and Wisitruangsakul, Nattwandee and Zebger, Ingo and Hildebrandt, Peter and Pereira, Manuela M. and Teixeira, Miguel and Murgida, Daniel H.
Pages 16952-16959
Year 2008
ISSN 1520-6106
DOI 10.1021/jp807862m
Address 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Journal J. Phys. Chem. B
Volume 112
Number 51
Month DEC 25
Publisher AMER CHEMICAL SOC
Abstract The cbb(3) oxygen reductase from Bradyrhizobium japonicum was immobilized on nanostructured silver electrodes by anchoring the enzyme via a His-tag to a Ni-NTA coating, followed by reconstitution of a lipid bilayer. The immobilized enzyme retains the native structure and catalytic activity as judged by in situ surface-enhanced vibrational spectroscopy and cyclic voltarnmetry, respectively. Spectroelectrochemical titrations followed by SERR spectroscopy of the integral enzyme and its monohemic (fixO) and dihemic subunits (fixP), allowed the determination of the reduction potentials for the different heme c groups. Both in the isolated subunits and in the integral enzyme the Met/His-coordinated hemes from the two subunits present identical reduction potentials of 180 mV, whereas for the bis-His heme from fixP the value is ca. 400 mV. The determination of reduction potentials of the individual hemes c reported in this work provides the basis for further exploring the mechanism of electroprotonic energy transduction of this complex enzyme.
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