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Related Concept Videos

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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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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.
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The Supercomplexes in the Crista Membrane01:41

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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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A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
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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.
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ATP Synthase: Structure01:18

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Modular structure of complex II: An evolutionary perspective.

Val Karavaeva1, Filipa L Sousa1

  • 1Department of Functional and Evolutionary Ecology, University of Vienna, Djerassiplatz 1, 1030 Wien, Austria.

Biochimica Et Biophysica Acta. Bioenergetics
|September 9, 2022
PubMed
Summary
This summary is machine-generated.

This study reveals that the evolutionary classification of succinate dehydrogenases (SDH) and fumarate reductases (FRD) aligns with structural types C, D, and F, but requires revision for types A, B, and E. A revised evolutionary model suggests a soluble precursor module diversifying through independent membrane anchor attachments.

Keywords:
Comparative genomicsElectron transport chainFumarate reductaseQuinol:Fumarate reductaseSuccinate dehydrogenaseSuccinate:Quinone oxidoreductase

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Area of Science:

  • Biochemistry and Molecular Biology
  • Evolutionary Biology
  • Genomics

Background:

  • Succinate dehydrogenases (SDH) and fumarate reductases (FRD) are crucial enzymes catalyzing the succinate-fumarate interconversion, conserved across all life.
  • Current SDH/FRD classification relies on membrane anchor subunit structure and cofactors, but its evolutionary validity is uncertain.

Purpose of the Study:

  • To investigate the evolutionary history and taxonomic distribution of succinate dehydrogenases and fumarate reductases.
  • To determine if structural classification of SDH/FRDs correlates with their phylogenetic relationships.

Main Methods:

  • Large-scale comparative genomic analysis of complex II.
  • Phylogenetic analysis of SDH/FRD enzyme families.

Main Results:

  • Structural classification aligns with phylogeny for SDH/FRD types C, D, and F.
  • Types A, B, and E exhibit a more complex evolutionary pattern, suggesting potential subgroups.
  • Evidence supports an evolutionary model with a primordial soluble module.

Conclusions:

  • A revised evolutionary scenario for SDH/FRDs is proposed, originating from a soluble precursor.
  • Independent membrane anchor attachment events likely drove the diversification of SDH/FRD diversity.
  • The study highlights the dynamic evolution of these essential enzyme complexes.