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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...
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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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Structural Isomerism

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Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
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Related Experiment Video

Updated: May 15, 2026

The Synthesis, Characterization and Reactivity of a Series of Ruthenium N-triphosPh Complexes
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Published on: April 10, 2015

Structural composition of alternative complex III: variations on the same theme.

Patrícia N Refojo1, Miguel A Ribeiro, Filipa Calisto

  • 1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República EAN, 2780-157 Oeiras, Portugal.

Biochimica Et Biophysica Acta
|January 15, 2013
PubMed
Summary
This summary is machine-generated.

Alternative complex III (ACIII) enzymes, involved in oxidoreductase activity, were found in more bacterial classes than previously known. Their diverse gene arrangements offer new insights into subunit functions like quinone binding and proton translocation.

Keywords:
ACIIIAlternative complex IIICISMCISM familyHeme copper oxygen reductaseRhodothermus marinusalternative complex IIIcomplex iron sulfur molybdoenzyme

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Isolation of Mitochondria for Mitochondrial Supercomplex Analysis from Small Tissue and Cell Culture Samples
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Isolation of Mitochondria for Mitochondrial Supercomplex Analysis from Small Tissue and Cell Culture Samples

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Last Updated: May 15, 2026

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Published on: April 10, 2015

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Isolation of Mitochondria for Mitochondrial Supercomplex Analysis from Small Tissue and Cell Culture Samples

Published on: May 3, 2024

Area of Science:

  • Biochemistry
  • Genomics
  • Microbiology

Background:

  • Alternative complex III (ACIII) is a recently identified enzyme family with quinol:electron acceptor oxidoreductase activity.
  • Initial studies indicated ACIII comprises six to eight subunits, with homology to known proteins.
  • The expanding availability of sequenced genomes prompted a re-evaluation of ACIII distribution.

Purpose of the Study:

  • To identify novel genes encoding ACIII subunits.
  • To investigate the diversity and organization of ACIII gene clusters across bacterial domains.
  • To gain new perspectives on ACIII subunit roles in quinone binding and proton translocation.

Main Methods:

  • Bioinformatic analysis of newly sequenced bacterial genomes.
  • Comparative genomics to identify ACIII gene clusters.
  • Analysis of gene cluster constitution and organization.

Main Results:

  • A larger number of ACIII gene clusters were identified, extending beyond previously known bacterial classes.
  • Significant diversity in the composition and organization of ACIII gene clusters was observed.
  • Unexpected gene arrangements provided new insights into subunit functions.

Conclusions:

  • ACIII enzymes are more widespread in bacteria than previously recognized.
  • The diversity in ACIII gene clusters suggests varied functional roles for its subunits.
  • Further research into ACIII structure and function is warranted, particularly concerning quinone binding and proton translocation.