Architecture of bacterial respiratory chains

VRI Kaila, M Wikström - Nature Reviews Microbiology, 2021 - nature.com
Bacteria power their energy metabolism using membrane-bound respiratory enzymes that
capture chemical energy and transduce it by pumping protons or Na+ ions across their cell …

[HTML][HTML] Metalloproteins containing cytochrome, iron–sulfur, or copper redox centers

J Liu, S Chakraborty, P Hosseinzadeh, Y Yu… - Chemical …, 2014 - ACS Publications
Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …

Biochemistry and theory of proton-coupled electron transfer

A Migliore, NF Polizzi, MJ Therien… - Chemical reviews, 2014 - ACS Publications
Through incremental change, Nature reworks and repurposes its functional machinery. In
this way, proteins that photochemically repair DNA by moving protons and electrons have a …

Catalysis and Electron Transfer in De Novo Designed Metalloproteins

KJ Koebke, TBJ Pinter, WC Pitts, VL Pecoraro - Chemical reviews, 2022 - ACS Publications
One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

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 …

Natural engineering principles of electron tunnelling in biological oxidation–reduction

CC Page, CC Moser, X Chen, PL Dutton - Nature, 1999 - nature.com
We have surveyed proteins with known atomic structure whose function involves electron
transfer; in these, electrons can travel up to 14 Å between redox centres through the protein …

The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å

T Tsukihara, H Aoyama, E Yamashita, T Tomizaki… - Science, 1996 - science.org
The crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution with an R
value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl …

Photochemical conversion of solar energy

V Balzani, A Credi, M Venturi - ChemSusChem: Chemistry & …, 2008 - Wiley Online Library
Energy is the most important issue of the 21st century. About 85% of our energy comes from
fossil fuels, a finite resource unevenly distributed beneath the Earth's surface. Reserves of …

Electrochemistry of redox-active self-assembled monolayers

AL Eckermann, DJ Feld, JA Shaw, TJ Meade - Coordination chemistry …, 2010 - Elsevier
Redox-active self-assembled monolayers (SAMs) provide an excellent platform for
investigating electron transfer kinetics. Using a well-defined bridge, a redox center can be …

Proton-coupled electron transfer in cytochrome oxidase

VRI Kaila, MI Verkhovsky, M Wikström - Chemical reviews, 2010 - ACS Publications
Enzyme reactions that involve strong coupling between proton and electron transfer are of
fundamental importance in biology. This is particularly evident in the reactions of primary …