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Evidence for Distinct Electron Transfer Processes in Terminal Oxidases from Different Origin by Means of Protein Film Voltammetry

MPG-Autoren
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Xie,  Hao
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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von der Hocht,  Iris
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Meyer, T., Melin, F., Xie, H., von der Hocht, I., Choi, S. K., Noor, M. R., et al. (2014). Evidence for Distinct Electron Transfer Processes in Terminal Oxidases from Different Origin by Means of Protein Film Voltammetry. Journal of the American Chemical Society, 136(31), 10821-11196. doi:10.1021/ja505126v.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0026-B1A7-F
Zusammenfassung
Cytochrome aa3 from Paracoccus denitrificans and cytochrome ba3 from Thermus thermophilus, two distinct members of the heme−copper oxidase superfamily, were immobilized on electrodes modified with gold nanoparticles. This procedure allowed us to achieve direct electron transfer between the enzyme and the gold nanoparticles and to obtain evidence for different electrocatalytic properties of the two enzymes. The pH dependence and thermostability reveal that the enzymes are highly adapted to their native environments. These results suggest that evolution resulted in different solutions to the common problem of electron transfer to oxygen.