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Related Concept Videos

ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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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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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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Mutations01:35

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Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
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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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Related Experiment Video

Updated: Apr 12, 2026

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase COX/SDH Double-labeling Histochemistry
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Structural and functional consequences of succinate dehydrogenase subunit B mutations.

E Kim1, E M Rath2, V H M Tsang3

  • 1Cancer GeneticsKolling Institute of Medical Research, Royal North Shore Hospital, and University of Sydney, Sydney, New South Wales, AustraliaDepartment of EndocrinologyRoyal North Shore Hospital, Sydney, New South Wales, AustraliaFaculty of PharmacyUniversity of Sydney, Sydney, New South Wales, AustraliaAustralian Nuclear Science and Technology OrganisationLucas Heights, New South Wales, Australia edward.kim@sydney.edu.au.

Endocrine-Related Cancer
|May 15, 2015
PubMed
Summary

Germline mutations in the succinate dehydrogenase B (SDHB) gene disrupt mitochondrial function, increasing cancer risk. This study uses structural modeling and in vitro assays to link specific SDHB mutations to impaired enzyme activity and cellular localization.

Keywords:
SDHBfunctional consequencesparagangliomaphaeochromocytomasuccinate dehydrogenase

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Area of Science:

  • Biochemistry
  • Genetics
  • Oncology

Background:

  • Mitochondrial dysfunction from succinate dehydrogenase (SDH) gene mutations is linked to various tumors, including phaeochromocytomas, paragangliomas, and renal cell carcinomas.
  • The precise mechanisms connecting germline SDH subunit B (SDHB) mutations to disease risk remain unclear.

Purpose of the Study:

  • To investigate the genotype-phenotype correlation of SDH subunit B (SDHB) variants.
  • To predict the biochemical effects of SDHB mutations using in silico methods.
  • To experimentally validate the functional consequences of SDHB mutations in vitro.

Main Methods:

  • Developed a homology model for human SDH based on crystallographic structures.
  • Mapped SDHB mutations and predicted their biochemical effects in silico.
  • Utilized GFP-tagged wild-type (WT) SDHB and mutant SDHB constructs transfected into HEK293 cells for in vitro functional assessment.

Main Results:

  • In silico predictions indicated that many SDHB mutations disrupt functional expression or electron transport.
  • Experimental results confirmed that specific SDHB mutations impair mitochondrial localization and/or SDH enzymatic activity.
  • Demonstrated a strong genotype-functional correlation for SDHB variants.

Conclusions:

  • Structural modeling effectively predicts the biological consequences of SDHB mutations.
  • Provides new insights into the functional impact of SDHB mutations.
  • Offers a valuable assay for distinguishing pathogenic SDHB mutations from benign variants, aiding in risk assessment for associated tumors.