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 …

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 …

There are two homologous membrane-bound enzymes in Escherichia coli that catalyze
reversible conversion between succinate/fumarate and quinone/quinol. Succinate …

Amino-acid selective isotope labeling of proteins offers numerous advantages in
mechanistic studies by revealing structural and functional information unattainable from a …

Cytochrome bo3 is the major respiratory oxidase located in the cytoplasmic membrane of
Escherichia coli when grown under high oxygen tension. The enzyme catalyzes the 2 …

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 …

Virtually all proton-pumping terminal respiratory oxygen reductases are members of the
heme-copper oxidoreductase superfamily. Most of these enzymes use reduced cytochrome …

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 …

Enrichment of proteins with isotopes such as 2 H, 15 N, and 13 C is commonly carried out in
magnetic resonance and vibrational spectroscopic characterization of protein structures …

Selective 15N isotope labeling of the cytochrome bo 3 ubiquinol oxidase from Escherichia
coli with auxotrophs was used to characterize the hyperfine couplings with the side-chain …