Redox tuning of cytochrome b562 through facile metal porphyrin substitution

Eduardo Antonio Della Pia; Qijin Chi; Martin Elliott; J. Emyr Macdonald; Jens Ulstrup; D. Dafydd Jones

doi:10.1039/C2CC34302A

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Redox tuning of cytochromeb₅₆₂ through facile metal porphyrin substitution†

Eduardo Antonio Della Pia,^ac Qijin Chi,*^b Martin Elliott,^c J. Emyr Macdonald,^c Jens Ulstrup^b and D. Dafydd Jones*^a

Author affiliations

* Corresponding authors

^a School of Biosciences, Main Building, Cardiff University, Cardiff CF10 3AT, UK
E-mail: jonesdd@cardiff.ac.uk

^b Department of Chemistry and NanoDTU, Technical University of Denmark, DK-2800 Lyngby, Denmark
E-mail: cq@kemi.dtu.dk

^c School of Physics and Astronomy, Queens' Building, Cardiff University, Cardiff CF24 3AA, UK

Abstract

The biologically and nanotechnologically important heme protein cytochrome b₅₆₂ was reconstructed with zinc and copper porphyrins, leading to significant changes in the spectral, redox and electron transfer properties. The Cu form shifts the redox potential by +300 mV and exhibits high electron transfer, while the Zn form is redox inert.

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Article information

DOI: https://doi.org/10.1039/C2CC34302A
Article type: Communication
Submitted: 15 Jun 2012
Accepted: 07 Sep 2012
First published: 07 Sep 2012

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Chem. Commun., 2012,48, 10624-10626

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Redox tuning of cytochrome b₅₆₂ through facile metal porphyrin substitution

E. A. D. Pia, Q. Chi, M. Elliott, J. Emyr Macdonald, J. Ulstrup and D. Dafydd Jones, Chem. Commun., 2012, 48, 10624 DOI: 10.1039/C2CC34302A

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Chemical Communications