Issue 31, 2020
From the journal:

Chemical Communications

Switching protein metalloporphyrin binding specificity by design from iron to fluorogenic zinc†

Benjamin J. Bowen, ORCID logo ‡a   Adam R. McGarrity,‡a   Jenn-Yeu A. Szeto,a   Christopher R. Pudney ORCID logo b  and  D. Dafydd Jones ORCID logo *a  

* Corresponding authors

a School of Biosciences, Cardiff University, Cardiff, UK
E-mail: jonesdd@cardiff.ac.uk

b Department of Biology and Biochemistry, University of Bath, Bath, UK

Abstract

Metalloporphyrins play important roles in areas ranging from biology to nanoscience. Using computational design, we converted metalloporphyrin specificity of cytochrome b562 from iron to fluorogenic zinc. The new variant had a near total preference for zinc representing a switch in specificity, which greatly enhanced the negligible aqueous fluorescence of free ZnPP in vitro and in vivo.

Graphical abstract: Switching protein metalloporphyrin binding specificity by design from iron to fluorogenic zinc

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Article information

DOI
https://doi.org/10.1039/D0CC00596G
Article type
Communication
Submitted
21 Jan 2020
Accepted
12 Mar 2020
First published
12 Mar 2020

Chem. Commun., 2020,56, 4308-4311

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Switching protein metalloporphyrin binding specificity by design from iron to fluorogenic zinc

B. J. Bowen, A. R. McGarrity, J. A. Szeto, C. R. Pudney and D. D. Jones, Chem. Commun., 2020, 56, 4308 DOI: 10.1039/D0CC00596G

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