Modulation of Functional Features in Electron Transferring Metalloproteins

REVIEW

DOI: https://doi.org/10.52712/sciencereviews.v1i2.18

Abstract

Electron transferring metalloproteins are typically implicated in shuttling electrons between energy transduction chains membrane complexes, such as in (aerobic and anaerobic) respiration and photosynthesis, among other functions. The thermodynamic and kinetic electron transfer parameters of the different metalloproteins need to be adjusted in each case to the specific demands, which can be quite diverse among organisms. Notably, biology utilizes very few metals, essentially iron and copper, to cover this broad range of redox needs imposed by biodiversity. Here, I will describe some crucial structural and dynamical characteristics that modulate the electron transfer parameters (and alternative functions) of two prototypical metalloproteins: the iron protein cytochrome c and its redox partner, the CuA center of the terminal respiratory enzyme cytochrome c oxidase. Specifically, I will focus on summarizing results obtained in recent years in my laboratory.

Author Biography

Daniel Horacio Murgida, Universidad de Buenos Aires (UBA)

Daniel H. Murgida received his PhD in Chemistry in 1997 from the School of Sciences of the University of Buenos Aires. He has been Visiting Scientist at the University of Parma, Humboldt Fellow at the Max Planck Institute for Radiation Chemistry, Staff Scientist at the New University of Lisbon, and Assistant Professor at the Technical University of Berlin. Since 2007 he is a Professor and CONICET Researcher at the University of Buenos Aires. His research focuses on structure-dynamicsfunction relationships that determine redox and alternative functions of metalloproteins, and combines theoretical and experimental approaches, mainly protein electrochemistry, spectroscopy and vibrational spectroelectrochemistry.

Published
2020-03-16
Issue
Vol 1 No 2: March 2020
Section
Articles