Redox tuning of cytochrome b562 through facile metal porphyrin substitution
Publication: Research - peer-review › Journal article – Annual report year: 2012
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Redox tuning of cytochrome b562 through facile metal porphyrin substitution. / Della Pia, Eduardo Antonio ; Chi, Qijin; Elliott, Martin; Macdonald, J. Emyr; Ulstrup, Jens; Jones, D. Dafydd .
In: Chemical Communications, Vol. 48, No. 86, 2012, p. 10624-10626.Publication: Research - peer-review › Journal article – Annual report year: 2012
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TY - JOUR
T1 - Redox tuning of cytochrome <em>b</em><sub>562</sub> through facile metal porphyrin substitution
A1 - Della Pia,Eduardo Antonio
A1 - Chi,Qijin
A1 - Elliott,Martin
A1 - Macdonald,J. Emyr
A1 - Ulstrup,Jens
A1 - Jones,D. Dafydd
AU - Della Pia,Eduardo Antonio
AU - Chi,Qijin
AU - Elliott,Martin
AU - Macdonald,J. Emyr
AU - Ulstrup,Jens
AU - Jones,D. Dafydd
PB - Royal Society of Chemistry
PY - 2012
Y1 - 2012
N2 - 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.<br/>
AB - 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.<br/>
U2 - 10.1039/c2cc34302a
DO - 10.1039/c2cc34302a
JO - Chemical Communications
JF - Chemical Communications
SN - 1359-7345
IS - 86
VL - 48
SP - 10624
EP - 10626
ER -