title: Redox tuning of cytochrome b562 through facile metal porphyrin substitution.
abstract: The biologically and nanotechnologically important heme protein cytochrome b(562) 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.
authors.affiliation: School of Biosciences, Main Building, Cardiff University, Cardiff CF10 3AT, UK.
authors.forename: Eduardo Antonio
authors.initials: EA
authors.lastname: Della Pia
authors.forename: Qijin
authors.initials: Q
authors.lastname: Chi
authors.forename: Martin
authors.initials: M
authors.lastname: Elliott
authors.forename: J Emyr
authors.initials: JE
authors.lastname: Macdonald
authors.forename: Jens
authors.initials: J
authors.lastname: Ulstrup
authors.forename: D Dafydd
authors.initials: DD
authors.lastname: Jones
mesh_terms: D003573:Cytochrome b Group / Q000737:chemistry* / Q000378:metabolism; D055664:Electrochemical Techniques; D004579:Electron Transport; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D011524:Protoporphyrins / Q000737:chemistry*
chemical_list: D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D011524:Protoporphyrins; C092553:copper protoporphyrin IX; C017803:zinc protoporphyrin; C017850:cytochrome b562, E coli