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

Cyanide-reactive sites in cytochrome bd complex from E. coli

I Krasnoselskaya1, A M Arutjunjan, I Smirnova

  • 1A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.

FEBS Letters
|August 2, 1993
PubMed
Summary

Cyanide interacts with E. coli cytochrome bd, causing heme d decomposition and a spin-state change in heme b595. This study demonstrates heme b595

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

The effect of synthesis conditions and process parameters on aerogel properties.

Frontiers in chemistry·2023
Same author

Micellization and Partition Equilibria in Mixed Nonionic/Ionic Micellar Systems: Predictions with Molecular Models.

Langmuir : the ACS journal of surfaces and colloids·2017
Same author

Solute Partitioning in Micelles: Combining Molecular Dynamics Simulations, COSMOmic, and Experiments.

The journal of physical chemistry. B·2017
Same author

Alginate-based hybrid aerogel microparticles for mucosal drug delivery.

European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V·2016
Same author

Molecular Modeling of Triton X Micelles: Force Field Parameters, Self-Assembly, and Partition Equilibria.

Journal of chemical theory and computation·2015
Same author

Polysaccharide-based aerogel microspheres for oral drug delivery.

Carbohydrate polymers·2014

Area of Science:

  • Biochemistry
  • Microbiology
  • Enzyme kinetics

Background:

  • Cytochrome bd is a key respiratory enzyme in E. coli.
  • Understanding its interaction with ligands is crucial for cellular respiration studies.

Purpose of the Study:

  • To investigate the reaction mechanism of cyanide with E. coli cytochrome bd.
  • To elucidate the role of heme b595 in ligand binding and spin-state transitions.

Main Methods:

  • Spectroscopic analysis (UV-Vis, MCD) to monitor spectral changes.
  • Kinetic studies to determine reaction rates and mechanisms.

Main Results:

  • Cyanide binding induces heme d oxycomplex decomposition and a Soret red shift in heme b595.
  • MCD spectra confirm a high-to-low spin transition for heme b595 upon cyanide binding.

Related Experiment Videos

  • Evidence suggests interaction between heme d and heme b595, with cyanide potentially acting as a bridging ligand.

    • Conclusions:

    • Heme b595 in cytochrome bd can bind exogenous ligands, a first-time demonstration.
    • The reaction kinetics suggest a coordinated response between heme d and heme b595.
    • Cyanide-induced spin-state transition in heme b595 is linked to heme d oxycomplex stability.