Biochemical Functions of Coenzyme Q10

  title={Biochemical Functions of Coenzyme Q10},
  author={Frederick L. Crane},
  journal={Journal of the American College of Nutrition},
  pages={591 - 598}
  • F. L. Crane
  • Published 1 December 2001
  • Biology, Chemistry
  • Journal of the American College of Nutrition
Coenzyme Q is well defined as a crucial component of the oxidative phosphorylation process in mitochondria which converts the energy in carbohydrates and fatty acids into ATP to drive cellular machinery and synthesis. New roles for coenzyme Q in other cellular functions are only becoming recognized. The new aspects have developed from the recognition that coenzyme Q can undergo oxidation/reduction reactions in other cell membranes such as lysosomes, Golgi or plasma membranes. In mitochondria… 


CoQ10’s cellular bioenergetic activity and antioxidant properties, and its functions for common clinical conditions such as cardiovascular and neurodegenerative diseases, cancer, diabetes, and renal failure are explored in this examination.

Calcium binding and transport by coenzyme Q.

It is shown that both CoQ10 and its analogue CoQ1, when exposed to CYP450 or alkaline media, undergo structural changes through a complex reaction pathway and form quinone structures with distinct properties, and electrochemically reduced forms of the new hydroxylated CoQs have higher antioxidative potential and are also able to bind and transport Ca(2+) across artificial biomimetic membranes.

Coenzyme Q 10 in the Human Retina

The relatively low levels of ubiquinone found in the bovine retina, coupled with the retina’s high levels of oxidative metabolism and its need for efficient lipid antioxidants, suggests that eye function may be sensitive to changes in CoQ10 concentrations.

Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms

  • M. Kawamukai
  • Biology, Chemistry
    Biotechnology and applied biochemistry
  • 2009
The present minireview focuses on the biochemical and commercial aspects of CoQ in yeasts and in other organisms for comparison.

Bioavailability of Ubiquinone versus Ubiquinol

This study evaluated plasma levels of circulating CoQ0 (both ubiquinone and ubiquinol) at baseline, four, six, and eight hours following a 300 mg dose of either USANA’s CoQuinone 100 or the equivalent dose of the leading competitor’'s ubiqu inol product.

Molecular genetics of ubiquinone biosynthesis in animals

The present knowledge of the eukaryotic biosynthesis of UQ is summarized, with focus on the biosynthetic genes identified in animals, including Caenorhabditis elegans, rodents, and humans, and the phenotypes of mutants in these genes are reviewed.

Mitochondrial function in cells, tissues and animals without ubiquinone biosynthesis

Liver mitochondrial function appears to have a high tolerance of severe UQ deficiency, and the respiratory phenotype of Mclk1 mutants can be considered essentially as a UQ-deficiency phenotype, and mitochondrial respiration can occur in the absence of UQ.

Coenzyme Q10 and Immune Function: An Overview

The aim of this article is to review the current literature available on both the role of Co Q10 in human immune function and the effect of CoQ10 supplementation on this system.

The molecular genetics of coenzyme Q biosynthesis in health and disease.

Biosynthesis, bioproduction and novel roles of ubiquinone.

  • M. Kawamukai
  • Biology, Chemistry
    Journal of bioscience and bioengineering
  • 2002



Expansion of antioxidant function of vitamin E by coenzyme Q

Recent studies in the laboratories have indicated that coenzyme Q and vitamin E, rather than acting independently in protecting biological membranes from oxidative attack, are integrated into a regenerative cycle.

Requirement for coenzyme Q in plasma membrane electron transport.

Evidence is consistent with a function for coenzyme Q in a trans-plasma membrane electron transport system which influences cell growth in rat hepatocyte and human erythrocyte plasma membranes.

Genetic Evidence for Coenzyme Q Requirement in Plasma Membrane Electron Transport

For the first time, genetic evidence is provided for the participation of ubiquinone in NADH–ascorbate free radical reductase, as a source of electrons for transmembrane ascorbate stabilization.

NADH and NADPH-dependent reduction of coenzyme Q at the plasma membrane.

The data presented here suggest that both nucleotides (NADH and NADPH) can be accountable for CoQ reduction by PMQR on the basis of their physiological concentrations within the cell.

Induction of endogenous coenzyme Q biosynthesis by administration of peroxisomal inducers

Administration of these drugs/chemicals to rats increased coenzyme Q levels in the blood and most of the organs and the extent of induction of this lipid was 8‐fold in young animals but decreased during aging and was absent at 1.5 year of age.

The existence of a lysosomal redox chain and the role of ubiquinone.

  • L. GilleH. Nohl
  • Biology, Chemistry
    Archives of biochemistry and biophysics
  • 2000
The experiments demonstrate a NADH-dependent reduction of UQ by two subsequent one-electron-transfer steps giving rise to the presence of ubisemiquinone and an increase of the ubiquinol pool in lysosomes, and demonstrate that this lipophilic electron carrier is a native constituent of a lyosomal electron transport chain, which promotes proton translocation across the lysOSomal membrane.

Role of plasma membrane coenzyme Q on the regulation of apoptosis

CoQ of the plasma membrane is suggested as a regulator of initiation phase of oxidative stress‐mediated serum withdrawal‐induced apoptosis and an inverse relationship between CoQ content in plasma membrane and lipid peroxidation rates in leukaemic cells is found.

Localization and mobility of coenzyme Q in lipid bilayers and membranes

It is concluded that CoQ diffusion is not rate‐limiting for electron transfer, since the experimental turnovers are independent of the distance between complexes.

Plasma membrane redox system in the control of stress-induced apoptosis.

The hypothesis that antioxidant protective function of the plasma membrane redox system can be enough to protect cells against the externally induced mild oxidative stress is proposed.