Blue Copper Proteins: A rigid machine for efficient electron transfer, a flexible device for metal uptake

Archives of Biochemistry and Biophysics
Sergio Alejo Pérez-HenarejosAntonio Donaire

Abstract

Blue Copper Proteins (BCPs) are small and generally soluble copper-containing proteins which participate in monoelectron transfer processes in biological systems. An overview of their electronic and tertiary structure is detailed here. The well-established entatic/rack-induced mechanism is explained by comparing thermodynamic parameters between the folded (tense) and the unfolded (relaxed) forms of the BCP rusticyanin. Recently, NMR solution data have shown that the active sites of BCPs in absence of the metal ion, i.e. in the apoforms, are flexible in the micro-to-second timescale. The rigidity proposed by the entatic/rack-induced mechanism is an imperative for the holoprotein to perform electron transfer; while the flexibility of the apocupredoxin is necessary to uptake the metal ion from the metallochaperones. These apparently contradictory requirements are discussed in the present work. Finally, the role of azurin and some peptides derived from it in anticancer therapy are also described.

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Citations

Dec 18, 2019·Current Pharmaceutical Design·Gesivaldo SantosDjalma M de Oliveira
May 29, 2020·Journal of Biomolecular Structure & Dynamics·Roghayeh JafarpourFaramarz Mehrnejad
Mar 15, 2019·IUCrJ·Diederik Johannes OppermanFelix Martín Ferroni
Dec 29, 2020·Frontiers in Microbiology·Javier Torregrosa-CrespoRosa María Martínez-Espinosa
Feb 23, 2021·Journal of Peptide Science : an Official Publication of the European Peptide Society·Siegmund Reissmann, Margarita P Filatova
Jul 18, 2017·Journal of the American Chemical Society·Alexandra V SoldatovaThomas G Spiro
Sep 22, 2021·The Journal of Physical Chemistry. B·Patrick Frank, Maurizio Benfatto
Dec 2, 2021·Journal of the American Chemical Society·Bang GongYong Huang
Nov 19, 2021·Metallomics : Integrated Biometal Science·Anne DurandSoufian Ouchane

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