Issue 24, 2020

CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential

Abstract

Attaining rational modulation of thermodynamic and kinetic redox parameters of metalloproteins is a key milestone towards the (re)design of proteins with new or improved redox functions. Here we report that implantation of ligand loops from natural T1 proteins into the scaffold of a CuA protein leads to a series of distorted T1-like sites that allow for independent modulation of reduction potentials (E°′) and electron transfer reorganization energies (λ). On the one hand E°′ values could be fine-tuned over 120 mV without affecting λ. On the other, λ values could be modulated by more than a factor of two while affecting E°′ only by a few millivolts. These results are in sharp contrast to previous studies that used T1 cupredoxin folds, thus highlighting the importance of the protein scaffold in determining such parameters.

Graphical abstract: CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential

Supplementary files

Article information

Article type
Edge Article
Submitted
18 Mär 2020
Accepted
01 Jun 2020
First published
01 Jun 2020
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2020,11, 6193-6201

CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential

J. Szuster, U. A. Zitare, M. A. Castro, A. J. Leguto, M. N. Morgada, A. J. Vila and D. H. Murgida, Chem. Sci., 2020, 11, 6193 DOI: 10.1039/D0SC01620A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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