Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

The bacterial cytochrome cbb3 oxidases.

Robert S Pitcher1, Nicholas J Watmough

  • 1Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.

Biochimica Et Biophysica Acta
|April 22, 2004
PubMed
Summary

Cytochrome cbb(3) oxidases, unique heme-copper oxidases in Proteobacteria, differ structurally from mitochondrial oxidases. Research explores their high oxygen affinity, varied electron inputs, and proton pumping abilities.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Regulation and Characterization of Mutants of <i>fixABCX</i> in <i>Rhizobium leguminosarum</i>.

Molecular plant-microbe interactions : MPMI·2021
Same author

Influence of the heme distal pocket on nitrite binding orientation and reactivity in Sperm Whale myoglobin.

The Biochemical journal·2021
Same author

Functional interactions between nitrite reductase and nitric oxide reductase from Paracoccus denitrificans.

Scientific reports·2019
Same author

Ultrafast Light-Driven Electron Transfer in a Ru(II)tris(bipyridine)-Labeled Multiheme Cytochrome.

Journal of the American Chemical Society·2019
Same author

Photosensitised Multiheme Cytochromes as Light-Driven Molecular Wires and Resistors.

Chembiochem : a European journal of chemical biology·2018
Same author

Tuning the modular Paracoccus denitrificans respirome to adapt from aerobic respiration to anaerobic denitrification.

Environmental microbiology·2017

Area of Science:

  • Biochemistry
  • Microbiology
  • Molecular Biology

Background:

  • Cytochrome cbb(3) oxidases are a distinct class of proton-pumping respiratory heme-copper oxidases (HCOs) found primarily in Proteobacteria.
  • They lack key structural features of the well-studied mitochondrial cytochrome c oxidase (CcO).
  • Their expression is crucial for pathogens colonizing anoxic tissues and for nitrogen fixation in diazotrophs.

Purpose of the Study:

  • To review recent advancements in the biochemical characterization of cytochrome cbb(3) oxidases.
  • To provide a foundation for understanding their unique properties, including high oxygen affinity and electron input pathways.
  • To investigate their capacity for proton pumping, potentially independent of other HCOs.

Main Methods:

  • Biochemical characterization techniques.

Related Experiment Videos

  • Comparative structural analysis.
  • Functional assays for oxygen affinity and proton pumping.

    • Main Results:

    • Recent studies have advanced the biochemical understanding of these oxidases.
    • Evidence suggests a high affinity for oxygen and diverse electron input mechanisms.
    • The independent proton pumping capability is under investigation.

    Conclusions:

    • Cytochrome cbb(3) oxidases possess unique biochemical and structural features compared to CcO.
    • Further research is needed to fully elucidate their functional mechanisms, particularly regarding proton pumping.
    • Understanding these oxidases is vital for applications in human health and agriculture.