Bacterial Oxidases of the Cytochrome bd Family: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets

VB Borisov, SA Siletsky, A Paiardini… - Antioxidants & redox …, 2021 - liebertpub.com
Significance: Cytochrome bd is a ubiquinol: oxygen oxidoreductase of many prokaryotic
respiratory chains with a unique structure and functional characteristics. Its primary role is to …

Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target

T Friedrich, D Wohlwend, VB Borisov - International Journal of Molecular …, 2022 - mdpi.com
Cytochrome bd is a triheme copper-free terminal oxidase in membrane respiratory chains of
prokaryotes. This unique molecular machine couples electron transfer from quinol to O2 with …

Homologous bd oxidases share the same architecture but differ in mechanism

A Theßeling, T Rasmussen, S Burschel… - Nature …, 2019 - nature.com
Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory
chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of …

Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D

A Grauel, J Kägi, T Rasmussen, I Makarchuk… - Nature …, 2021 - nature.com
Cytochrome bd quinol: O2 oxidoreductases are respiratory terminal oxidases so far only
identified in prokaryotes, including several pathogenic bacteria. Escherichia coli contains …

Features of Organization and Mechanism of Catalysis of Two Families of Terminal Oxidases: Heme-Copper and bd-Type

VB Borisov, SA Siletsky - Biochemistry (Moscow), 2019 - Springer
Terminal oxidases of aerobic respiratory chains catalyze the transfer of electrons from the
respiratory substrate, cytochrome c or quinol, to O 2 with the formation of two H 2 O …

[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

E Forte, VB Borisov, SA Siletsky, M Petrosino… - … et Biophysica Acta (BBA …, 2019 - Elsevier
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 …

Features and Functional Importance of Key Residues of the Mycobacterium tuberculosis Cytochrome bd Oxidase

E Sviriaeva, MS Subramanian Manimekalai… - ACS Infectious …, 2020 - ACS Publications
Cytochrome bd (cyt-bd) oxygen reductases have a high affinity to oxygen and use the two
electrons provided by ubiquinol or menaquinol, like in mycobacteria, to reduce oxygen to …

Proton transfer in cytochrome bd-I from E. coli involves Asp-105 in CydB

M Janczak, J Vilhjálmsdóttir, P Ädelroth - Biochimica et Biophysica Acta …, 2024 - Elsevier
Cytochrome bds are bacterial terminal oxidases expressed under low oxygen conditions,
and they are important for the survival of many pathogens and hence potential drug targets …

Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms

A Nikolaev, S Safarian, A Thesseling… - … et Biophysica Acta (BBA …, 2021 - Elsevier
Cytochrome bd oxidase is a bacterial terminal oxygen reductase that was suggested to
enable adaptation to different environments and to confer resistance to stress conditions. An …

An engineered glutamate in biosynthetic models of heme-copper oxidases drives complete product selectivity by tuning the hydrogen-bonding network

ID Petrik, R Davydov, M Kahle, B Sandoval… - Biochemistry, 2021 - ACS Publications
Efficiently carrying out the oxygen reduction reaction (ORR) is critical for many applications
in biology and chemistry, such as bioenergetics and fuel cells, respectively. In biology, this …