Cytochrome bd and Gaseous Ligands in Bacterial Physiology

Elena Forte, Vitaliy B. Borisov, João B. Vicente, Alessandro Giuffrè

Research output: Chapter in Book/Report/Conference proceedingChapter

11 Citations (Scopus)

Abstract

Cytochrome bd is a unique prokaryotic respiratory terminal oxidase that does not belong to the extensively investigated family of haem–copper oxidases (HCOs). The enzyme catalyses the four-electron reduction of O2 to 2H2O, using quinols as physiological reducing substrates. The reaction is electrogenic and cytochrome bd therefore sustains bacterial energy metabolism by contributing to maintain the transmembrane proton motive force required for ATP synthesis. As compared to HCOs, cytochrome bd displays several distinctive features in terms of (i) metal composition (it lacks Cu and harbours a d-type haem in addition to two haems b), (ii) overall three-dimensional structure, that only recently has been solved, and arrangement of the redox cofactors, (iii) lesser energetic efficiency (it is not a proton pump), (iv) higher O2 affinity, (v) higher resistance to inhibitors such as cyanide, nitric oxide (NO) and hydrogen sulphide (H2S) and (vi) ability to efficiently metabolize potentially toxic reactive oxygen and nitrogen species like hydrogen peroxide (H2O2) and peroxynitrite (ONOO). Compelling evidence suggests that, beyond its bioenergetic role, cytochrome bd plays multiple functions in bacterial physiology and affords protection against oxidative and nitrosative stress. Relevant to human pathophysiology, thanks to its peculiar properties, the enzyme has been shown to promote virulence in several bacterial pathogens, being currently recognized as a target for the development of new antibiotics. This review aims to give an update on our current understanding of bd-type oxidases with a focus on their reactivity with gaseous ligands and its potential impact on bacterial physiology and human pathophysiology.

Original languageEnglish
Title of host publicationAdvances in Microbial Physiology
PublisherAcademic Press
Pages171-234
Number of pages64
Volume71
DOIs
Publication statusPublished - 1 Jan 2017

Publication series

NameAdvances in Microbial Physiology
Volume71
ISSN (Print)0065-2911

Fingerprint

Bacterial Physiological Phenomena
Cytochromes
Oxidoreductases
Ligands
Heme
Energy Metabolism
Hydroquinones
Reactive Nitrogen Species
Proton Pumps
Hydrogen Sulfide
Proton-Motive Force
Peroxynitrous Acid
Poisons
Cyanides
Electron Transport Complex IV
Enzymes
Hydrogen Peroxide
Oxidation-Reduction
Virulence
Reactive Oxygen Species

Keywords

  • Bacterial respiratory chain
  • Gaseous signalling molecules
  • Haem protein
  • Oxidative and nitrosative stress
  • Pathogenic bacteria
  • Terminal oxidase
  • Virulence

Cite this

Forte, E., Borisov, V. B., Vicente, J. B., & Giuffrè, A. (2017). Cytochrome bd and Gaseous Ligands in Bacterial Physiology. In Advances in Microbial Physiology (Vol. 71, pp. 171-234). (Advances in Microbial Physiology; Vol. 71). Academic Press. https://doi.org/10.1016/bs.ampbs.2017.05.002
Forte, Elena ; Borisov, Vitaliy B. ; Vicente, João B. ; Giuffrè, Alessandro. / Cytochrome bd and Gaseous Ligands in Bacterial Physiology. Advances in Microbial Physiology. Vol. 71 Academic Press, 2017. pp. 171-234 (Advances in Microbial Physiology).
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Forte, E, Borisov, VB, Vicente, JB & Giuffrè, A 2017, Cytochrome bd and Gaseous Ligands in Bacterial Physiology. in Advances in Microbial Physiology. vol. 71, Advances in Microbial Physiology, vol. 71, Academic Press, pp. 171-234. https://doi.org/10.1016/bs.ampbs.2017.05.002

Cytochrome bd and Gaseous Ligands in Bacterial Physiology. / Forte, Elena; Borisov, Vitaliy B.; Vicente, João B.; Giuffrè, Alessandro.

Advances in Microbial Physiology. Vol. 71 Academic Press, 2017. p. 171-234 (Advances in Microbial Physiology; Vol. 71).

Research output: Chapter in Book/Report/Conference proceedingChapter

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T1 - Cytochrome bd and Gaseous Ligands in Bacterial Physiology

AU - Forte, Elena

AU - Borisov, Vitaliy B.

AU - Vicente, João B.

AU - Giuffrè, Alessandro

PY - 2017/1/1

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N2 - Cytochrome bd is a unique prokaryotic respiratory terminal oxidase that does not belong to the extensively investigated family of haem–copper oxidases (HCOs). The enzyme catalyses the four-electron reduction of O2 to 2H2O, using quinols as physiological reducing substrates. The reaction is electrogenic and cytochrome bd therefore sustains bacterial energy metabolism by contributing to maintain the transmembrane proton motive force required for ATP synthesis. As compared to HCOs, cytochrome bd displays several distinctive features in terms of (i) metal composition (it lacks Cu and harbours a d-type haem in addition to two haems b), (ii) overall three-dimensional structure, that only recently has been solved, and arrangement of the redox cofactors, (iii) lesser energetic efficiency (it is not a proton pump), (iv) higher O2 affinity, (v) higher resistance to inhibitors such as cyanide, nitric oxide (NO) and hydrogen sulphide (H2S) and (vi) ability to efficiently metabolize potentially toxic reactive oxygen and nitrogen species like hydrogen peroxide (H2O2) and peroxynitrite (ONOO−). Compelling evidence suggests that, beyond its bioenergetic role, cytochrome bd plays multiple functions in bacterial physiology and affords protection against oxidative and nitrosative stress. Relevant to human pathophysiology, thanks to its peculiar properties, the enzyme has been shown to promote virulence in several bacterial pathogens, being currently recognized as a target for the development of new antibiotics. This review aims to give an update on our current understanding of bd-type oxidases with a focus on their reactivity with gaseous ligands and its potential impact on bacterial physiology and human pathophysiology.

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KW - Bacterial respiratory chain

KW - Gaseous signalling molecules

KW - Haem protein

KW - Oxidative and nitrosative stress

KW - Pathogenic bacteria

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KW - Virulence

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Forte E, Borisov VB, Vicente JB, Giuffrè A. Cytochrome bd and Gaseous Ligands in Bacterial Physiology. In Advances in Microbial Physiology. Vol. 71. Academic Press. 2017. p. 171-234. (Advances in Microbial Physiology). https://doi.org/10.1016/bs.ampbs.2017.05.002