Catalytic Reactions and Energy Conservation in the Cytochrome bc1 and b6f Complexes of Energy-Transducing Membranes

M Sarewicz, S Pintscher, R Pietras, A Borek… - Chemical …, 2021 - ACS Publications
This review focuses on key components of respiratory and photosynthetic energy-
transduction systems: the cytochrome bc 1 and b 6 f (Cyt bc 1/b 6 f) membranous …

Redox properties of the membrane proteins from the respiratory chain

F Melin, P Hellwig - Chemical reviews, 2020 - ACS Publications
This review focuses on the electrochemical and spectroelectrochemical studies that gave
insight into redox potentials of the four mitochondrial complexes and their homologues from …

Evolution of quinol oxidation within the heme‑copper oxidoreductase superfamily

R Murali, J Hemp, RB Gennis - Biochimica et Biophysica Acta (BBA) …, 2022 - Elsevier
The heme‑copper oxidoreductase (HCO) superfamily is a large superfamily of terminal
respiratory enzymes that are widely distributed across the three domains of life. The …

Cryo-EM structures of Escherichia coli cytochrome bo3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site

J Li, L Han, F Vallese, Z Ding, SK Choi… - Proceedings of the …, 2021 - National Acad Sciences
Two independent structures of the proton-pumping, respiratory cytochrome bo 3 ubiquinol
oxidase (cyt bo 3) have been determined by cryogenic electron microscopy (cryo-EM) in …

Oxygen as acceptor

VB Borisov, MI Verkhovsky - EcoSal Plus, 2015 - Am Soc Microbiol
Like most bacteria, Escherichia coli has a flexible and branched respiratory chain that
enables the prokaryote to live under a variety of environmental conditions, from highly …

High-frequency and-field electron paramagnetic resonance of transition metal ion (d block) coordination complexes

J Telser, A Ozarowski, J Krzystek - Electron Paramagnetic …, 2012 - books.google.com
High-frequency and-field electron paramagnetic resonance (HFEPR), in its current
configuration (frequencies up to 1THz; fields up to 35T), has been applied to transition metal …

Structure of the cytochrome aa3-600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site

J Xu, Z Ding, B Liu, SM Yi, J Li… - Proceedings of the …, 2020 - National Acad Sciences
Virtually all proton-pumping terminal respiratory oxygen reductases are members of the
heme-copper oxidoreductase superfamily. Most of these enzymes use reduced cytochrome …

Prediction of high- and low-affinity quinol-analogue-binding sites in the aa3 and bo3 terminal oxidases from Bacillus subtilis and Escherichia coli

F Bossis, A De Grassi, LL Palese… - Biochemical …, 2014 - portlandpress.com
Haem–copper oxidases are the terminal enzymes in both prokaryotic and eukaryotic
respiratory chains. They catalyse the reduction of dioxygen to water and convert redox …

In Situ Spectroelectrochemical Investigations of the Redox-Active Tris[4-(pyridin-4-yl)phenyl]amine Ligand and a Zn2+ Coordination Framework

C Hua, A Baldansuren, F Tuna, D Collison… - Inorganic …, 2016 - ACS Publications
An investigation of the redox-active tris [4-(pyridin-4-yl) phenyl] amine (NPy3) ligand in the
solution state and upon its incorporation into the solid-state metal–organic framework …

Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli

SK Choi, L Schurig-Briccio, Z Ding… - Journal of the …, 2017 - ACS Publications
Cytochrome bo 3 is a respiratory proton-pumping oxygen reductase that is a member of the
heme-copper superfamily that utilizes ubiquinol-8 (Q8H2) as a substrate. The current …