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

Haem-polypeptide interactions during cytochrome c maturation.

L Thöny-Meyer1

  • 1Institute of Microbiology, ETH Zürich, Schmelzbergstrasse 7, CH-8092, Zürich, Switzerland. lthoeny@micro.biol.ethz.ch

Biochimica Et Biophysica Acta
|September 27, 2000
PubMed
Summary

This review details the journey of haem, a crucial cofactor, during cytochrome c maturation in Escherichia coli. Key proteins like CcmC, CcmE, and CcmF facilitate haem trafficking and covalent attachment to apocytochrome.

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

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

Biochemical Society transactions·2002
Same author

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

Acta crystallographica. Section D, Biological crystallography·2001

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Cytochrome c maturation requires the coordinated translocation and ligation of apocytochrome and its haem cofactor across a membrane.
  • The process is best understood in the Gram-negative bacterium Escherichia coli, involving a series of proteinaceous maturation factors.

Purpose of the Study:

  • To review the current understanding of haem's journey during cytochrome c maturation.
  • To elucidate the roles of specific cytochrome c maturation (Ccm) proteins in haem trafficking.

Main Methods:

  • This study is a review article, synthesizing existing research on cytochrome c maturation.
  • Focuses on the known interactions and proposed functions of Ccm proteins involved in haem binding and transfer.

Related Experiment Videos

Main Results:

  • Haem passage and ligation are mediated by Ccm proteins, with CcmC, CcmE, and CcmF interacting directly with haem.
  • CcmE acts as a haem-binding intermediate, CcmC facilitates haem binding to CcmE, and CcmF mediates release and transfer to apocytochrome.
  • The precise mechanism of haem translocation across the cytoplasmic membrane remains undetermined.

Conclusions:

  • The Ccm protein machinery plays a critical role in guiding haem during cytochrome c maturation.
  • Further investigation is needed to fully understand the membrane translocation step of haem.
  • Elucidating these mechanisms is vital for understanding bacterial respiration and protein biogenesis.