Synthetic Fe/Cu complexes: toward understanding heme-copper oxidase structure and function
Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …
Impact of hydrogen sulfide on mitochondrial and bacterial bioenergetics
VB Borisov, E Forte - International Journal of Molecular Sciences, 2021 - mdpi.com
This review focuses on the effects of hydrogen sulfide (H2S) on the unique bioenergetic
molecular machines in mitochondria and bacteria—the protein complexes of electron …
molecular machines in mitochondria and bacteria—the protein complexes of electron …
A 'Build and Retrieve'methodology to simultaneously solve cryo-EM structures of membrane proteins
Single-particle cryo-electron microscopy (cryo-EM) has become a powerful technique in the
field of structural biology. However, the inability to reliably produce pure, homogeneous …
field of structural biology. However, the inability to reliably produce pure, homogeneous …
Redox properties of the membrane proteins from the respiratory chain
This review focuses on the electrochemical and spectroelectrochemical studies that gave
insight into redox potentials of the four mitochondrial complexes and their homologues from …
insight into redox potentials of the four mitochondrial complexes and their homologues from …
Cryo-EM structures of Escherichia coli cytochrome bo3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site
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 …
oxidase (cyt bo 3) have been determined by cryogenic electron microscopy (cryo-EM) in …
Terminal Oxidase Cytochrome bd Protects Bacteria Against Hydrogen Sulfide Toxicity
VB Borisov, E Forte - Biochemistry (Moscow), 2021 - Springer
Hydrogen sulfide (H 2 S) is often called the third gasotransmitter (after nitric oxide and
carbon monoxide), or endogenous gaseous signaling molecule. This compound plays …
carbon monoxide), or endogenous gaseous signaling molecule. This compound plays …
Short-chain aurachin D derivatives are selective inhibitors of E. coli cytochrome bd-I and bd-II oxidases
M Radloff, I Elamri, TN Grund, LF Witte, KF Hohmann… - Scientific Reports, 2021 - nature.com
Cytochrome bd-type oxidases play a crucial role for survival of pathogenic bacteria during
infection and proliferation. This role and the fact that there are no homologues in the …
infection and proliferation. This role and the fact that there are no homologues in the …
[HTML][HTML] In the respiratory chain of Escherichia coli cytochromes bd-I and bd-II are more sensitive to carbon monoxide inhibition than cytochrome bo3
Bacteria can not only encounter carbon monoxide (CO) in their habitats but also produce the
gas endogenously. Bacterial respiratory oxidases, thus, represent possible targets for CO …
gas endogenously. Bacterial respiratory oxidases, thus, represent possible targets for CO …
In Escherichia coli Ammonia Inhibits Cytochrome bo3 But Activates Cytochrome bd-I
E Forte, SA Siletsky, VB Borisov - Antioxidants, 2020 - mdpi.com
Interaction of two redox enzymes of Escherichia coli, cytochrome bo 3 and cytochrome bd-I,
with ammonium sulfate/ammonia at pH 7.0 and 8.3 was studied using high-resolution …
with ammonium sulfate/ammonia at pH 7.0 and 8.3 was studied using high-resolution …
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 …
heme-copper oxidoreductase superfamily. Most of these enzymes use reduced cytochrome …