Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

D Alvarez-Paggi, L Hannibal, MA Castro… - Chemical …, 2017 - ACS Publications
Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible
structure, particularly in the ferric form, such that it is able to sample a broad conformational …

Redox properties of heme peroxidases

G Battistuzzi, M Bellei, CA Bortolotti, M Sola - Archives of biochemistry and …, 2010 - Elsevier
Peroxidases are heme enzymes found in bacteria, fungi, plants and animals, which exploit
the reduction of hydrogen peroxide to catalyze a number of oxidative reactions, involving a …

Engineered proteins: redox properties and their applications

S Prabhulkar, H Tian, X Wang, JJ Zhu… - Antioxidants & redox …, 2012 - liebertpub.com
Oxidoreductases and metalloproteins, representing more than one third of all known
proteins, serve as significant catalysts for numerous biological processes that involve …

The Reversible Opening of Water Channels in Cytochrome c Modulates the Heme Iron Reduction Potential

CA Bortolotti, A Amadei, M Aschi… - Journal of the …, 2012 - ACS Publications
Dynamic protein–solvent interactions are fundamental for life processes, but their
investigation is still experimentally very demanding. Molecular dynamics simulations up to …

The enthalpic and entropic terms of the reduction potential of metalloproteins: Determinants and interplay

G Di Rocco, G Battistuzzi, M Borsari… - Coordination Chemistry …, 2021 - Elsevier
Splitting the reduction potential of electron transport (ET) proteins and redox
metalloenzymes into the enthalpic and entropic contributions is an insightful practice to …

The Reorganization Energy in Cytochrome c is Controlled by the Accessibility of the Heme to the Solvent

CA Bortolotti, ME Siwko, E Castellini… - The Journal of …, 2011 - ACS Publications
Elucidation of the molecular determinants of the reorganization energy λ is central to the
understanding of fundamental biological processes based on energy transduction …

Adsorbing surface strongly influences the pseudoperoxidase and nitrite reductase activity of electrode-bound yeast cytochrome c. The effect of hydrophobic …

L Lancellotti, M Borsari, A Bonifacio, CA Bortolotti… - …, 2020 - Elsevier
Abstract The Met80Ala and Met80Ala/Tyr67Ala variants of S. cerevisiae iso-1 cytochrome c
(ycc) and their adducts with cardiolipin immobilized onto a gold electrode coated with a …

Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c

D Alvarez-Paggi, MA Castro, V Tórtora… - Journal of the …, 2013 - ACS Publications
We have employed a combination of protein film voltammetry, time-resolved vibrational
spectroelectrochemistry and molecular dynamics simulations to evaluate the electron …

Urea-induced denaturation of immobilized yeast iso-1 cytochrome c: Role of Met80 and Tyr67 in the thermodynamics of unfolding and promotion of pseudoperoxidase …

L Lancellotti, M Borsari, M Bellei, A Bonifacio… - Electrochimica …, 2020 - Elsevier
Abstract The Met80Ala and Met80Ala/Tyr67Ala variants of S. cerevisiae iso-1 cytochrome c
(ycc) immobilized on a decane-1-thiol coated gold electrode subjected to the denaturing …

Electron Transfer Properties and Hydrogen Peroxide Electrocatalysis of Cytochrome c Variants at Positions 67 and 80

S Casalini, G Battistuzzi, M Borsari… - The Journal of …, 2010 - ACS Publications
Replacement of the axial Met80 heme ligand in electrode-immobilized cytochrome c with a
noncoordinating Ala residue and alteration of the hydrogen bonding network in the region …