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Updated: Jul 9, 2025

Assessment of Cellular Oxidation using a Subcellular Compartment-Specific Redox-Sensitive Green Fluorescent Protein

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Published on: June 18, 2020

[Cytochrome bd as Antioxidant Redox Enzyme].

V B Borisov^1,2, M R Nastasi³, E Forte³

¹Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119991 Russia.

Molekuliarnaia Biologiia

|December 8, 2023

Summary

Cytochrome bd oxidases in E. coli not only maintain redox balance but also eliminate harmful hydrogen peroxide. These findings highlight their dual role in bacterial cellular health and antioxidant defense.

Keywords:

Escherichia coli cytochrome bd heme hydrogen peroxide oxidative stress reactive oxygen species redox enzyme respiratory chain terminal oxidase

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Published on: November 23, 2011

Area of Science:

Microbiology
Biochemistry
Cellular Respiration

Background:

Electron transport chains maintain cellular redox homeostasis.
Cytochrome bd is a unique terminal oxidase in bacteria, coupling ubiquinol/menaquinol oxidation to proton motive force generation for ATP production.
Escherichia coli possesses two bd-type oxidases: bd-I (cydAB) and bd-II (appCB).

Conclusions:

Cytochrome bd oxidases possess a dual function: energy generation and reactive oxygen species detoxification.
The H2O2-scavenging activity of these enzymes is a significant, previously underappreciated, aspect of bacterial physiology.
Further research is warranted to explore the broader implications of these antioxidant properties in microbial communities.