Multifunctional Cytochrome c: Learning New Tricks from an Old Dog
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 …
structure, particularly in the ferric form, such that it is able to sample a broad conformational …
[HTML][HTML] Electrochemistry of surface-confined enzymes: Inspiration, insight and opportunity for sustainable biotechnology
Highlights•New strategies for enzyme electrochemistry.•Recent applications of enzyme
electrochemistry.•Synergies of fundamental and applied enzyme electrochemistry.Redox …
electrochemistry.•Synergies of fundamental and applied enzyme electrochemistry.Redox …
Thermodynamics of metalloprotein electron transfer reactions
VT Taniguchi, N Sailasuta-Scott, FC Anson… - Pure and Applied …, 1980 - degruyter.com
Thin—layer spectroelectrochemical methods have been used to determine the formal
reduction potentials of several electron transfer metalloproteins in the temperature range 5 …
reduction potentials of several electron transfer metalloproteins in the temperature range 5 …
Semisynthetic and biomolecular hydrogen evolution catalysts
There has been great interest in the development of stable, inexpensive, efficient catalysts
capable of reducing aqueous protons to hydrogen (H2), an alternative to fossil fuels. While …
capable of reducing aqueous protons to hydrogen (H2), an alternative to fossil fuels. While …
The enthalpic and entropic terms of the reduction potential of metalloproteins: Determinants and interplay
Splitting the reduction potential of electron transport (ET) proteins and redox
metalloenzymes into the enthalpic and entropic contributions is an insightful practice to …
metalloenzymes into the enthalpic and entropic contributions is an insightful practice to …
How to turn an electron transfer protein into a redox enzyme for biosensing
Cytochrome c is a small globular protein whose main physiological role is to shuttle
electrons within the mitochondrial electron transport chain. This protein has been widely …
electrons within the mitochondrial electron transport chain. This protein has been widely …
Towards Bacterial Resistance via the Membrane Strategy: Enzymatic, Biophysical and Biomimetic Studies of the Lipid cis‐trans Isomerase of Pseudomonas …
M Mauger, I Makarchuk, Y Molter, A Sansone… - …, 2024 - Wiley Online Library
The lipid cis‐trans isomerase (Cti) is a periplasmic heme‐c enzyme found in several
bacteria including Pseudomonas aeruginosa, a pathogen known for causing nosocomial …
bacteria including Pseudomonas aeruginosa, a pathogen known for causing nosocomial …
Determining Redox Potentials of the Iron–Sulfur Clusters of the AdoMet Radical Enzyme Superfamily
SJ Maiocco, LM Walker, SJ Elliott - Methods in Enzymology, 2018 - Elsevier
While protein film electrochemistry (PFE) has proven to be an effective tool in the
interrogation of redox cofactors and assessing the electrocatalytic activity of many different …
interrogation of redox cofactors and assessing the electrocatalytic activity of many different …
Effect of motional restriction on the unfolding properties of a cytochrome c featuring a His/Met–His/His ligation switch
Abstract The K72A/K73H/K79A variant of cytochrome c undergoes a reversible change from
a His/Met to a His/His axial heme ligation upon urea-induced unfolding slightly below …
a His/Met to a His/His axial heme ligation upon urea-induced unfolding slightly below …
Methionine Ligand Lability of Homologous Monoheme Cytochromes c
Direct electrochemical analysis of adsorbed bacterial monoheme cytochromes c has
revealed a phenomenological loss of the axial methionine when examined using pyrolytic …
revealed a phenomenological loss of the axial methionine when examined using pyrolytic …