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

Cytochrome c maturation: a complex pathway for a simple task?

L Thöny-Meyer1

  • 1Institut für Mikrobiologie, Departement Biologie, ETH Zentrum, CH-8092 Zürich, Switzerland. lthoeny@micro.biol.ethz.ch

Biochemical Society Transactions
|August 28, 2002
PubMed
Summary

The study details the complex process of c-type cytochrome maturation in bacteria, focusing on heme attachment. It reveals how heme delivery and thio-reduction pathways merge for stereospecific heme insertion into apocytochrome c.

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

Protection of wood from microorganisms by laccase-catalyzed iodination.

Applied and environmental microbiology·2012
Same author

Efficient production of Al(OH)3-immobilized laccase with a Heterobasidion annosum strain selected by microplate screening.

Journal of applied microbiology·2011
Same author

Isolation and purification of medium chain length poly(3-hydroxyalkanoates) (mcl-PHA) for medical applications using nonchlorinated solvents.

Biomacromolecules·2010
Same author

Expression and crystallization of DsbA from Staphylococcus aureus.

Acta crystallographica. Section F, Structural biology and crystallization communications·2007
Same author

Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE).

Acta crystallographica. Section D, Biological crystallography·2001
Same author

Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation.

The Journal of biological chemistry·2001

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Post-translational maturation of c-type cytochromes requires covalent heme attachment.
  • In bacteria like Escherichia coli, this process occurs in the periplasm involving a complex protein system.

Purpose of the Study:

  • To elucidate the mechanisms of heme delivery and attachment to apocytochrome c.
  • To understand the roles of specific proteins and pathways in cytochrome c maturation.

Main Methods:

  • Investigated the translocation of heme and apocytochrome c across the cytoplasmic membrane.
  • Characterized the heme attachment to the chaperone CcmE and subsequent transfer to apocytochrome c.
  • Examined the thio-reduction pathway involving thioredoxin, DsbD, CcmG/CcmH, and reductases.

Related Experiment Videos

Main Results:

  • Heme attachment to CcmE is transient, involving integral membrane proteins CcmC and CcmF.
  • Apocytochrome c requires reduction of cysteine residues in a Cys-Xaa-Xaa-Cys-His motif before heme binding.
  • The heme delivery and thio-reduction pathways converge for stereospecific heme insertion.

Conclusions:

  • The study clarifies the intricate, multi-protein machinery essential for c-type cytochrome biogenesis.
  • Understanding these pathways is crucial for comprehending bacterial electron transport and cellular respiration.