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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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...
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...
Skeleton and Calcium Homeostasis01:21

Skeleton and Calcium Homeostasis

Calcium is not only the most abundant mineral in bone but also the most abundant mineral in the human body. Calcium ions are needed for bone mineralization, tooth health, heart rate regulation and strength of contraction, blood coagulation, the contraction of smooth and skeletal muscle cells, and the regulation of nerve impulse conduction. The average calcium level in the blood is about 10 mg/dL. When the body cannot maintain this level, a person will experience hypo or hypercalcemia.
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Feedback Regulation of Calcium Concentration

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

Calcium binding and transport by coenzyme Q.

Ivan Bogeski1, Rubin Gulaboski, Reinhard Kappl

  • 1Department of Biophysics, School of Medicine, Saarland University, 66421 Homburg, Germany.

Journal of the American Chemical Society
|May 10, 2011
PubMed
Summary

Coenzyme Q10 (CoQ10) undergoes structural changes via Cytochrome P450 enzymes, forming hydroxylated forms with enhanced antioxidant capacity and calcium-binding abilities, impacting mitochondrial function.

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Area of Science:

  • Mitochondrial biochemistry
  • Enzyme kinetics
  • Biophysical chemistry

Background:

  • Coenzyme Q10 (CoQ10) is vital for mitochondrial electron transport chain (ETC) and ATP production.
  • Cytochrome P450 (CYP450) enzymes, present in the inner mitochondrial membrane, modify compounds.
  • The interaction between CYP450 and CoQ10 and its impact on mitochondrial function remain unexplored.

Purpose of the Study:

  • To investigate the interaction between CoQ10/CoQ1 and CYP450.
  • To elucidate the structural modifications of CoQ10/CoQ1 upon interaction.
  • To assess the functional consequences of these modifications on mitochondrial homeostasis.

Main Methods:

  • Voltammetry
  • UV-vis spectrometry
  • Electron paramagnetic resonance (EPR)
  • Nuclear magnetic resonance (NMR)
  • Fluorescence microscopy
  • High-performance liquid chromatography-mass spectrometry (HPLC-MS)

Main Results:

  • CoQ10 and CoQ1 undergo structural changes when exposed to CYP450 or alkaline conditions.
  • These changes involve the replacement of methoxy groups with hydroxyl groups, forming novel quinone structures.
  • The resulting hydroxylated CoQ forms exhibit increased antioxidative potential and Ca(2+) transport capabilities.
  • These modified CoQ forms can bind and transport Ca(2+) across artificial biomimetic membranes.

Conclusions:

  • CYP450 enzymes can structurally modify CoQ10 and its analogues.
  • Hydroxylated CoQ forms possess altered biochemical properties, including enhanced antioxidant and Ca(2+) transport functions.
  • These findings suggest a novel regulatory role for CoQ10 and its derivatives in mitochondrial Ca(2+) and redox homeostasis.