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Related Concept Videos

Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

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...
Electron Transport Chains01:28

Electron Transport Chains

The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
Photosystem I01:27

Photosystem I

Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
Photosystem II01:22

Photosystem II

The multi-protein complex photosystem II (PS II) harvests photons and transfers their energy through its bound pigments to its reaction center, and ultimately to photosystem I (PSI) through the electron transport chain. The pigments responsible for caputirng the light energy in photosystems include chlorophyll a, chlorophyll b, and carotenoids.
The pigment molecules are arranged across  two photosystem domains — the antenna complex and the reaction center. The main aim of the pigment molecules...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

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Related Experiment Video

Updated: May 29, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

Cytochrome c biogenesis System I.

Julie M Stevens1, Despoina A I Mavridou, Rebecca Hamer

  • 1Department of Biochemistry, University of Oxford, Oxford, UK.

The FEBS Journal
|October 1, 2011
PubMed
Summary
This summary is machine-generated.

Cytochrome c maturation involves a complex system for heme attachment. This study details the multiprotein cytochrome c maturation (Ccm) System I in Escherichia coli, crucial for forming essential thioether bonds.

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A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
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A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

Related Experiment Videos

Last Updated: May 29, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Cytochromes c are vital respiratory proteins requiring heme attachment.
  • Heme attachment involves forming two thioether bonds between cysteine residues and heme vinyl groups.
  • This reaction does not occur spontaneously due to unactivated heme vinyl groups.

Purpose of the Study:

  • To describe the complex multiprotein cytochrome c maturation (Ccm) system, also known as System I.
  • To elucidate the mechanism of heme attachment in Escherichia coli via the Ccm System I.
  • To detail the protein components (CcmABCDEFGH) involved in System I.

Main Methods:

  • Detailed analysis of the cytochrome c maturation (Ccm) system in Escherichia coli.
  • Identification and characterization of the CcmABCDEFGH protein complex.
  • Investigation of the post-translational modification pathway for heme attachment.

Main Results:

  • The cytochrome c maturation (Ccm) System I in E. coli is a complex multiprotein system.
  • This system, comprising CcmABCDEFGH proteins, is responsible for heme attachment to cytochromes c.
  • The study outlines the specific roles of proteins within System I in forming the necessary thioether bonds.

Conclusions:

  • The Ccm System I is essential for the physiological formation of c-type cytochromes in E. coli.
  • Understanding this system provides insight into diverse post-translational modification mechanisms.
  • System I represents a conserved pathway found in plant mitochondria, archaea, and Gram-negative bacteria.