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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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Related Experiment Video

Updated: Jun 14, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
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Published on: July 20, 2022

Cytochrome c biogenesis: the Ccm system.

Carsten Sanders1, Serdar Turkarslan, Dong-Woo Lee

  • 1Kutztown University, Department of Biology, Kutztown, PA 19530, USA.

Trends in Microbiology
|April 13, 2010
PubMed
Summary

Cytochrome c maturation (Ccm) systems attach heme groups to proteins via thioether bonds. This study reveals functional interactions within Ccm components, explaining the molecular basis of heme attachment in c-type cytochromes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Cytochromes c are essential proteins containing covalently attached heme groups.
  • Heme attachment involves thioether bonds formed between heme b vinyl groups and cysteine residues in apocytochromes.
  • Cytochrome c maturation (Ccm) systems, particularly the complex System I, are crucial for this post-translational modification in various organisms.

Purpose of the Study:

  • To elucidate the functional interactions among components of the Ccm system.
  • To provide a mechanistic understanding of the molecular basis for heme b-apocytochrome thioether bond formation.
  • To detail the ubiquitous vinyl-2 approximately Cys(1) and vinyl-4 approximately Cys(2) linkages in c-type cytochromes.

Main Methods:

  • Analysis of emerging functional interactions between Ccm components.
  • Categorization of Ccm components into three conserved modules.
  • Mechanistic investigation of thioether bond formation.

Main Results:

  • Identification of conserved functional interactions within the Ccm system.
  • Detailed mechanistic insights into the formation of vinyl-2 approximately Cys(1) and vinyl-4 approximately Cys(2) thioether bonds.
  • Understanding the molecular basis of heme attachment across diverse organisms.

Conclusions:

  • The Ccm system's components interact functionally to facilitate heme attachment.
  • A mechanistic view of thioether bond formation provides insight into c-type cytochrome biogenesis.
  • This work enhances understanding of essential post-translational modifications in diverse life forms.