Bacterial Oxidases of the CytochromebdFamily: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets Article Swipe
Vitaliy B. Borisov
,
Sergey A. Siletsky
,
Alessandro Paiardini
,
David Hoogewijs
,
Elena Forte
,
Alessandro Giuffrè
,
Robert K. Poole
·
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1089/ars.2020.8039
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1089/ars.2020.8039
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 couple the reduction of molecular oxygen, even at submicromolar concentrations, to water with the generation of a proton motive force used for adenosine triphosphate production. Cytochrome bd is found in many bacterial pathogens and, surprisingly, in bacteria formally denoted as anaerobes. It endows bacteria with resistance to various stressors and is a potential drug target. Recent Advances: We summarize recent advances in the biochemistry, structure, and physiological functions of cytochrome bd in the light of exciting new three-dimensional structures of the oxidase. The newly discovered roles of cytochrome bd in contributing to bacterial protection against hydrogen peroxide, nitric oxide, peroxynitrite, and hydrogen sulfide are assessed. Critical Issues: Fundamental questions remain regarding the precise delineation of electron flow within this multihaem oxidase and how the extraordinarily high affinity for oxygen is accomplished, while endowing bacteria with resistance to other small ligands. Future Directions: It is clear that cytochrome bd is unique in its ability to confer resistance to toxic small molecules, a property that is significant for understanding the propensity of pathogens to possess this oxidase. Since cytochrome bd is a uniquely bacterial enzyme, future research should focus on harnessing fundamental knowledge of its structure and function to the development of novel and effective antibacterial agents.
Related Topics
Concepts
Biochemistry
Ubiquinol
Cytochrome
Cytochrome c oxidase
Cytochrome c
Bacteria
Chemistry
Respiratory chain
Biology
Oxidase test
Enzyme
Coenzyme Q – cytochrome c reductase
Mitochondrion
Genetics
Metadata
- Type
- review
- Language
- en
- Landing Page
- https://doi.org/10.1089/ars.2020.8039
- OA Status
- green
- Cited By
- 101
- References
- 355
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W3086092904
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W3086092904Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1089/ars.2020.8039Digital Object Identifier
- Title
-
Bacterial Oxidases of the CytochromebdFamily: Redox Enzymes of Unique Structure, Function, and Utility As Drug TargetsWork title
- Type
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reviewOpenAlex work type
- Language
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enPrimary language
- Publication year
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2020Year of publication
- Publication date
-
2020-09-14Full publication date if available
- Authors
-
Vitaliy B. Borisov, Sergey A. Siletsky, Alessandro Paiardini, David Hoogewijs, Elena Forte, Alessandro Giuffrè, Robert K. PooleList of authors in order
- Landing page
-
https://doi.org/10.1089/ars.2020.8039Publisher landing page
- Open access
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YesWhether a free full text is available
- OA status
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greenOpen access status per OpenAlex
- OA URL
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https://www.ncbi.nlm.nih.gov/pmc/articles/8112716Direct OA link when available
- Concepts
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Biochemistry, Ubiquinol, Cytochrome, Cytochrome c oxidase, Cytochrome c, Bacteria, Chemistry, Respiratory chain, Biology, Oxidase test, Enzyme, Coenzyme Q – cytochrome c reductase, Mitochondrion, GeneticsTop concepts (fields/topics) attached by OpenAlex
- Cited by
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101Total citation count in OpenAlex
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2025: 29, 2024: 31, 2023: 22, 2022: 8, 2021: 8Per-year citation counts (last 5 years)
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355Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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