Coenzyme Q10

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Coenzyme Q10
Coenzyme Q10.svg
Names
Preferred IUPAC name
2-[(2E,6E,10E,14E,18E,22E,26E,30E,34E)-3,7,11,15,19,23,27,31,35,39-Decamethyltetraconta-2,6,10,14,18,22,26,30,34,38-decaen-1-yl]-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione
Other names
  • In general: Ubiquinone, coenzyme Q, CoQ, vitamin Q
  • This form: ubidecarenone,

Q10, CoQ10 /ˌkoʊˌkjuːˈtɛn/

Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.005.590 OOjs UI icon edit-ltr-progressive.svg
KEGG
PubChem CID
UNII
  • InChI=1S/C59H90O4/c1-44(2)24-15-25-45(3)26-16-27-46(4)28-17-29-47(5)30-18-31-48(6)32-19-33-49(7)34-20-35-50(8)36-21-37-51(9)38-22-39-52(10)40-23-41-53(11)42-43-55-54(12)56(60)58(62-13)59(63-14)57(55)61/h24,26,28,30,32,34,36,38,40,42H,15-23,25,27,29,31,33,35,37,39,41,43H2,1-14H3/b45-26+,46-28+,47-30+,48-32+,49-34+,50-36+,51-38+,52-40+,53-42+ Yes check.svgY
    Key: ACTIUHUUMQJHFO-UPTCCGCDSA-N Yes check.svgY
  • InChI=1/C59H90O4/c1-44(2)24-15-25-45(3)26-16-27-46(4)28-17-29-47(5)30-18-31-48(6)32-19-33-49(7)34-20-35-50(8)36-21-37-51(9)38-22-39-52(10)40-23-41-53(11)42-43-55-54(12)56(60)58(62-13)59(63-14)57(55)61/h24,26,28,30,32,34,36,38,40,42H,15-23,25,27,29,31,33,35,37,39,41,43H2,1-14H3/b45-26+,46-28+,47-30+,48-32+,49-34+,50-36+,51-38+,52-40+,53-42+
    Key: ACTIUHUUMQJHFO-UPTCCGCDBK
  • O=C1/C(=C(\C(=O)C(\OC)=C1\OC)C)C\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)C
Properties
C59H90O4
Molar mass 863.365 g·mol−1
Appearanceyellow or orange solid
Melting point 48–52 °C (118–126 °F; 321–325 K)
insoluble
Pharmacology
C01EB09 ( WHO )
Related compounds
Related quinones
1,4-Benzoquinone
Plastoquinone
Ubiquinol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Yes check.svgY  verify  (what is  Yes check.svgYX mark.svgN ?)

Coenzyme Q10 (CoQ10 /ˌkoʊkjuːˈtɛn/ ) also known as ubiquinone, is a naturally occurring biochemical cofactor (coenzyme) and an antioxidant produced by the human body. [1] [2] [3] It can also be obtained from dietary sources, such as meat, fish, seed oils, vegetables, and dietary supplements. [1] [2] CoQ10 is found in many organisms, including animals and bacteria.

CoQ10 plays a role in mitochondrial oxidative phosphorylation, aiding in the production of adenosine triphosphate (ATP), which is involved in energy transfer within cells. [1] The structure of CoQ10 consists of a benzoquinone moiety and an isoprenoid side chain, with the "10" referring to the number of isoprenyl chemical subunits in its tail. [4] [5] [6]

Although a ubiquitous molecule in human tissues, CoQ10 is not a dietary nutrient and does not have a recommended intake level, and its use as a supplement is not associated with or approved for any health or anti-disease effect. [1] [2]

Biological functions

CoQ10 is a component of the mitochondrial electron transport chain (ETC), where it plays a role in oxidative phosphorylation, a process required for the biosynthesis of adenosine triphosphate, the primary energy source of cells. [1] [6] [7]

CoQ10 is a lipophilic molecule that is located in all biological membranes of human body and serves as a component for the synthesis of ATP and is a life-sustaining cofactor for the three complexes (complex I, complex II, and complex III) of the ETC in the mitochondria. [1] [5] CoQ10 has a role in the transport of protons across lysosomal membranes to regulate pH in lysosome functions. [1]

The mitochondrial oxidative phosphorylation process takes place in the inner mitochondrial membrane of eukaryotic cells. [1] This membrane is highly folded into structures called cristae, which increase the surface area available for oxidative phosphorylation. CoQ10 plays a role in this process as an essential cofactor of the ETC located in the inner mitochondrial membrane and serves the following functions: [1] [7]

CoQ10 also may influence immune response by modulating the expression of genes involved in inflammation. [10] [11] [12]

Biochemistry

Coenzymes Q is a coenzyme family that is ubiquitous in animals and many Pseudomonadota, [13] a group of gram-negative bacteria. The fact that the coenzyme is ubiquitous gives the origin of its other name, ubiquinone. [1] [2] [14] In humans, the most common form of coenzymes Q is coenzyme Q10, also called CoQ10 ( /ˌkoʊkjuːˈtɛn/ ) or ubiquinone-10. [1]

Coenzyme Q10 is a 1,4-benzoquinone, in which "Q" refers to the quinone chemical group and "10" refers to the number of isoprenyl chemical subunits (shown enclosed in brackets in the diagram) in its tail. [1] In natural ubiquinones, there are from six to ten subunits in the tail, with humans having a tail of 10 isoprene units (50 carbon atoms) connected to its benzoquinone "head". [1]

This family of fat-soluble substances is present in all respiring eukaryotic cells, primarily in the mitochondria. [1] Ninety-five percent of the human body's energy is generated this way. [15] Organs with the highest energy requirements—such as the heart, liver, and kidney—have the highest CoQ10 concentrations. [16] [17] [18] [19]

There are three redox states of CoQ: fully oxidized (ubiquinone), semiquinone (ubisemiquinone), and fully reduced (ubiquinol). [1] The capacity of this molecule to act as a two-electron carrier (moving between the quinone and quinol form) and a one-electron carrier (moving between the semiquinone and one of these other forms) is central to its role in the electron transport chain due to the iron–sulfur clusters that can only accept one electron at a time, and as a free radical–scavenging antioxidant. [1] [14]

Deficiency

There are two major pathways of deficiency of CoQ10 in humans: reduced biosynthesis, and increased use by the body. [10] [20] Biosynthesis is the major source of CoQ10. Biosynthesis requires at least 15 genes, and mutations in any of them can cause CoQ deficiency. [20] CoQ10 levels also may be affected by other genetic defects (such as mutations of mitochondrial DNA, ETFDH , APTX , FXN , and BRAF , genes that are not directly related to the CoQ10 biosynthetic process). [20] Some of these, such as mutations in COQ6 , can lead to serious diseases such as steroid-resistant nephrotic syndrome with sensorineural deafness. [21] [22] [23]

Assessment

Although CoQ10 may be measured in blood plasma, these measurements reflect dietary intake rather than tissue status. Currently, most clinical centers measure CoQ10 levels in cultured skin fibroblasts, muscle biopsies, and blood mononuclear cells. [24] Culture fibroblasts can be used also to evaluate the rate of endogenous CoQ10 biosynthesis, by measuring the uptake of 14C-labeled p-hydroxybenzoate. [25]

Statins

Although statins may reduce CoQ10 in the blood it is unclear if they reduce CoQ10 in muscle. [26] Evidence does not support that supplementation improves side effects from statins. [26] [27]

Chemical properties

The oxidized structure of CoQ10 is shown below. The various kinds of coenzyme Q may be distinguished by the number of isoprenoid subunits in their side-chains. The most common coenzyme Q in human mitochondria is CoQ10. [1] Q refers to the quinone head and "10" refers to the number of isoprene repeats in the tail. The molecule below has three isoprenoid units and would be called Q3.

Unibuinone3.svg

In its pure state, it is an orange-colored lipophile powder, and has no taste nor odor. [14]

Biosynthesis

Biosynthesis occurs in most human tissue. There are three major steps:

  1. Creation of the benzoquinone structure (using phenylalanine or tyrosine, via 4-hydroxybenzoate)
  2. Creation of the isoprene side chain (using acetyl-CoA)
  3. The joining or condensation of the above two structures

The initial two reactions occur in mitochondria, the endoplasmic reticulum, and peroxisomes, indicating multiple sites of synthesis in animal cells. [28]

An important enzyme in this pathway is HMG-CoA reductase, usually a target for intervention in cardiovascular complications. The "statin" family of cholesterol-reducing medications inhibits HMG-CoA reductase. One possible side effect of statins is decreased production of CoQ10, which may be connected to the development of myopathy and rhabdomyolysis. However, the role statins play in CoQ deficiency is controversial. Although statins reduce blood levels of CoQ, studies on the effects of muscle levels of CoQ are yet to come. CoQ supplementation also does not reduce side effects of statin medications. [24] [26]

Genes involved include PDSS1 , PDSS2 , COQ2 , and ADCK3 (COQ8, CABC1). [29]

Organisms other than humans produce the benzoquinone and isoprene structures from somewhat different source chemicals. For example, the bacteria E. coli produces the former from chorismate and the latter from a non-mevalonate source. The common yeast S. cerevisiae , however, derives the former from either chorismate or tyrosine and the latter from mevalonate. Most organisms share the common 4-hydroxybenzoate intermediate, yet again uses different steps to arrive at the "Q" structure. [30]

Dietary supplement

Although neither a prescription drug nor an essential nutrient, CoQ10 is commonly used as a dietary supplement with the intent to prevent or improve disease conditions, such as cardiovascular disorders. [2] [31] CoQ10 is naturally produced by the body and plays a crucial role in cell growth and protection. [6] Despite its significant role in the body, it is not used as a drug for the treatment of any specific disease. [1] [2] [3]

Nevertheless, CoQ10 is widely available as an over-the-counter dietary supplement and is recommended by some healthcare professionals, despite a lack of definitive scientific evidence supporting these recommendations, [1] [3] especially when it comes to cardiovascular diseases. [32]

Regulation and composition

CoQ10 is not approved by the U.S. Food and Drug Administration (FDA) for the treatment of any medical condition. [33] [34] [35] [36] However, it is sold as a dietary supplement not subject to the same regulations as medicinal drugs, and is an ingredient in some cosmetics. [37] The manufacture of CoQ10 is not regulated, and different batches and brands may vary significantly. [35]

Research

A 2014 Cochrane review found insufficient evidence to make a conclusion about its use for the prevention of heart disease. [38] A 2016 Cochrane review concluded that CoQ10 had no effect on blood pressure. [39] A 2021 Cochrane review found "no convincing evidence to support or refute" the use of CoQ10 for the treatment of heart failure. [40]

A 2017 meta-analysis of people with heart failure taking 30–100 mg/d of CoQ10 found a 31% lower mortality and increased exercise capacity, with no significant difference in the endpoints of left heart ejection fraction. [41] A 2021 meta-analysis found that coenzyme Q10 was associated with a 31% lower all-cause mortality in HF patients. [42] In a 2023 meta-analysis of older people, ubiquinone had evidence of a cardiovascular effect, but ubiquinol did not. [43]

Although CoQ10 has been studied as a potential remedy to treat purported muscle-related side effects of statin medications, the results were mixed. Although a 2018 meta-analysis concluded that there was preliminary evidence for oral CoQ10 reducing statin-associated muscle symptoms, including muscle pain, muscle weakness, muscle cramps and muscle tiredness, [44] 2015 [45] and 2024 [32] meta-analysis found that CoQ10 had no effect on statin myopathy. [45] [32]

Pharmacology

Absorption

CoQ10 in the pure form is a crystalline powder insoluble in water. Absorption as a pharmacological substance follows the same process as that of lipids; the uptake mechanism appears to be similar to that of vitamin E, another lipid-soluble nutrient. [19] This process in the human body involves secretion into the small intestine of pancreatic enzymes and bile, which facilitates emulsification and micelle formation required for absorption of lipophilic substances. [46] Food intake (and the presence of lipids) stimulates bodily biliary excretion of bile acids and greatly enhances absorption of CoQ10. Exogenous CoQ10 is absorbed from the small intestine and is best absorbed if taken with a meal. Serum concentration of CoQ10 in fed condition is higher than in fasting conditions. [47] [48]

Metabolism

CoQ10 is metabolized in all tissues, with the metabolites being phosphorylated in cells. [2] CoQ10 is reduced to ubiquinol during or after absorption in the small intestine. [2] It is absorbed by chylomicrons, and redistributed in the blood within lipoproteins. [2] Its elimination occurs via biliary and fecal excretion. [2]

Pharmacokinetics

Some reports have been published on the pharmacokinetics of CoQ10. The plasma peak can be observed 6–8 hours after oral administration when taken as a pharmacological substance. [2] In some studies, a second plasma peak also was observed at approximately 24 hours after administration, probably due to both enterohepatic recycling and redistribution from the liver to circulation. [46]

Deuterium-labeled crystalline CoQ10 was used to investigate pharmacokinetics in humans to determine an elimination half-time of 33 hours. [49]

Bioavailability

In contrast to intake of CoQ10 as a constituent of food, such as nuts or meat, from which CoQ10 is normally absorbed, there is a concern about CoQ10 bioavailability when it is taken as a dietary supplement. [50] [51] Bioavailability of CoQ10 supplements may be reduced due to the lipophilic nature of its molecule and large molecular weight. [50]

Reduction of particle size

Nanoparticles have been explored as a delivery system for various drugs, such as improving the oral bioavailability of drugs with poor absorption characteristics. [52] However, this has not proved successful with CoQ10, although reports have differed widely. [53] [54] The use of aqueous suspension of finely powdered CoQ10 in pure water also reveals only a minor effect. [55]

Water-solubility

Facilitating drug absorption by increasing its solubility in water is a common pharmaceutical strategy and also has been shown to be successful for CoQ10. Various approaches have been developed to achieve this goal, with many of them producing significantly better results over oil-based softgel capsules in spite of the many attempts to optimize their composition. [19] Examples of such approaches are use of the aqueous dispersion of solid CoQ10 with the polymer tyloxapol, [56] formulations based on various solubilising agents, such as hydrogenated lecithin, [57] and complexation with cyclodextrins; among the latter, the complex with β-cyclodextrin has been found to have highly increased bioavailability [58] [59] and also is used in pharmaceutical and food industries for CoQ10-fortification. [19]

Adverse effects and precautions

Generally, oral CoQ10 supplementation is well tolerated. [1] The most common side effects are gastrointestinal symptoms (nausea, vomiting, appetite suppression, and abdominal pain), rashes, and headaches. [60] Some adverse effects, largely gastrointestinal, are reported with intakes. [2] Doses of 100–300 mg per day may induce insomnia or elevate liver enzymes. [2] The observed safe level risk assessment method indicated that the evidence of safety is acceptable at intakes up to 1200 mg per day. [61]

Use of CoQ10 supplementation is not recommended in people with liver or kidney disease, during pregnancy or breastfeeding, or in the elderly. [2]

Potential drug interactions

CoQ10 taken as a pharmacological substance has potential to inhibit the effects of theophylline as well as the anticoagulant warfarin; CoQ10 may interfere with warfarin's actions by interacting with cytochrome p450 enzymes thereby reducing the INR, a measure of blood clotting. [62] The structure of CoQ10 is similar to that of vitamin K, which competes with and counteracts warfarin's anticoagulation effects. CoQ10 is not recommended in people taking warfarin due to the increased risk of clotting. [60]

Dietary concentrations

Detailed reviews on occurrence of CoQ10 and dietary intake were published in 2010. [63] Besides the endogenous synthesis within organisms, CoQ10 also is supplied by various foods. [1] CoQ10 concentrations in various foods are: [1]

CoQ10 levels in selected foods [63]
FoodCoQ10 concentration (mg/kg)
Vegetable oils soybean oil 54–280
olive oil 40–160
grapeseed oil 64–73
sunflower oil 4–15
canola oil 64–73
Beefheart113
liver39–50
muscle26–40
Porkheart12–128
liver23–54
muscle14–45
Chickenbreast8–17
thigh24–25
wing11
Fish sardine 5–64
mackerel – red flesh43–67
mackerel – white flesh11–16
salmon 4–8
tuna 5
Nuts peanut 27
walnut 19
sesame seed 18–23
pistachio 20
hazelnut 17
almond 5–14
Vegetables parsley 8–26
broccoli 6–9
cauliflower 2–7
spinach up to 10
Chinese cabbage 2–5
Fruit avocado 10
blackcurrant 3
grape 6–7
strawberry 1
orange 1–2
grapefruit 1
apple 1
banana 1

Vegetable oils, meat and fish are quite rich in CoQ10 levels. [1] Dairy products are much poorer sources of CoQ10 than animal tissues. Among vegetables, broccoli and cauliflower are good sources of CoQ10. [1] Most fruit and berries are poor sources of CoQ10, with the exception of avocados, which have a relatively high oil and CoQ10 content. [63]

Intake

In the developed world, the estimated daily intake of CoQ10 has been determined at 3–6 mg per day, derived primarily from meat. [63]

South Koreans have an estimated average daily CoQ (Q9 + Q10) intake of 11.6 mg/d, derived primarily from kimchi. [64]

Effect of heat and processing

Cooking by frying reduces CoQ10 content by 14–32%. [65]

History

In 1950, a small amount of CoQ10 was isolated from the lining of a horse's gut, a compound initially called substance SA, but later deemed to be quinone found in many animal tissues. [66] In 1957, the same compound was isolated from mitochondrial membranes of beef heart, with research showing that it transported electrons within mitochondria. It was called Q-275 as a quinone. [66] [67] The Q-275/substance SA was later renamed ubiquinone as it was a ubiquitous quinone found in all animal tissues. [66] In 1958, its full chemical structure was reported. [66] [68] Ubiquinone was later called either mitoquinone or coenzyme Q due to its participation to the mitochondrial electron transport chain. [66] In 1966, a study reported that reduced CoQ6 was an effective antioxidant in cells. [69]

See also

Related Research Articles

<span class="mw-page-title-main">Oxidative phosphorylation</span> Metabolic pathway

Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.

<span class="mw-page-title-main">Respiratory complex I</span> Protein complex involved in cellular respiration

Respiratory complex I, EC 7.1.1.2 is the first large protein complex of the respiratory chains of many organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and translocates protons across the inner mitochondrial membrane in eukaryotes or the plasma membrane of bacteria.

<span class="mw-page-title-main">Coenzyme Q – cytochrome c reductase</span> Class of enzymes

The coenzyme Q : cytochrome c – oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain, playing a critical role in biochemical generation of ATP. Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial and the nuclear genomes. Complex III is present in the mitochondria of all animals and all aerobic eukaryotes and the inner membranes of most bacteria. Mutations in Complex III cause exercise intolerance as well as multisystem disorders. The bc1 complex contains 11 subunits, 3 respiratory subunits, 2 core proteins and 6 low-molecular weight proteins.

<span class="mw-page-title-main">Succinate dehydrogenase</span> Enzyme

Succinate dehydrogenase (SDH) or succinate-coenzyme Q reductase (SQR) or respiratory complex II is an enzyme complex, found in many bacterial cells and in the inner mitochondrial membrane of eukaryotes. It is the only enzyme that participates in both the citric acid cycle and oxidative phosphorylation. Histochemical analysis showing high succinate dehydrogenase in muscle demonstrates high mitochondrial content and high oxidative potential.

<span class="mw-page-title-main">Ubiquinol</span> Chemical compound

A ubiquinol is an electron-rich (reduced) form of coenzyme Q (ubiquinone). The term most often refers to ubiquinol-10, with a 10-unit tail most commonly found in humans.

<span class="mw-page-title-main">MT-ND5</span> Mitochondrial gene coding for a protein involved in the respiratory chain

MT-ND5 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 5 protein (ND5). The ND5 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Variations in human MT-ND5 are associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS) as well as some symptoms of Leigh's syndrome and Leber's hereditary optic neuropathy (LHON).

<span class="mw-page-title-main">PDSS1</span> Protein-coding gene in the species Homo sapiens

Decaprenyl-diphosphate synthase subunit 1 is an enzyme that in humans is encoded by the PDSS1 gene.

<span class="mw-page-title-main">COQ2</span> Protein-coding gene in humans

Para-hydroxybenzoate—polyprenyltransferase, mitochondrial is an enzyme that in humans is encoded by the COQ2 gene.

<span class="mw-page-title-main">ETFDH</span> Protein-coding gene in humans

Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial is an enzyme that in humans is encoded by the ETFDH gene. This gene encodes a component of the electron-transfer system in mitochondria and is essential for electron transfer from a number of mitochondrial flavin-containing dehydrogenases to the main respiratory chain.

<span class="mw-page-title-main">NADH:ubiquinone reductase (non-electrogenic)</span> Class of enzymes

NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with systematic name NADH:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction:

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<span class="mw-page-title-main">NDUFB3</span> Protein-coding gene in the species Homo sapiens

NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 3, 12kDa is a protein that in humans is encoded by the NDUFB3 gene. NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 3, 12kDa is an accessory subunit of the NADH dehydrogenase (ubiquinone) complex, located in the mitochondrial inner membrane. It is also known as Complex I and is the largest of the five complexes of the electron transport chain. Mutations in this gene contribute to mitochondrial complex I deficiency.

<span class="mw-page-title-main">NDUFA3</span> Protein-coding gene in the species Homo sapiens

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 is a protein that in humans is encoded by the NDUFA3 gene. The NDUFA3 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.

<span class="mw-page-title-main">NDUFAB1</span> Protein-coding gene in the species Homo sapiens

NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 5, 16kDa is a protein that in humans is encoded by the NDUFAB1 gene. The NDUFAB1 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.

William V. Judy, Ph.D. was an American author, clinical researcher, clinical trial consultant, and retired professor of physiology and biophysics. He was first introduced to the field of Coenzyme Q10 clinical research by Karl Folkers, the American bio-chemist who determined the structure of the Coenzyme Q10 molecule. 

<span class="mw-page-title-main">International Coenzyme Q10 Association</span>

The International Coenzyme Q10 Association is a nonprofit association originally based in Ancona, Italy and currently in Seville, Spain. Since its establishment in 1997, it has promoted biochemical and clinical research on the substance Coenzyme Q10 in an attempt to increase the body of knowledge about the preventive and therapeutic health effects of Coenzyme Q10.

<span class="mw-page-title-main">Plácido Navas Lloret</span> Spanish Professor of Cell Biology

Plácido Navas Lloret is a Spanish Professor of Cell Biology in the Andalusian Center for Developmental Biology at the Pablo de Olavide University in Sevilla, Spain. From 2002 to 2012, Professor Navas served as a board member of the International Coenzyme Q10 Association; since 2013, he has been the chairman of the association.

<span class="mw-page-title-main">Mitoquinone mesylate</span> Chemical compound

Mitoquinone mesylate (MitoQ) is a synthetic analogue of coenzyme Q10 which has antioxidant effects. It was first developed in New Zealand in the late 1990s. It has significantly improved bioavailability and improved mitochondrial penetration compared to coenzyme Q10, and has shown potential in a number of medical indications, being widely sold as a dietary supplement.

<span class="mw-page-title-main">Coenzyme Q5, methyltransferase</span> Enzyme found in humans

Coenzyme Q5, methyltransferase, more commonly known as COQ5, is an enzyme involved in the electron transport chain. COQ5 is located within the mitochondrial matrix and is a part of the biosynthesis of ubiquinone.

Probico also known as PBCo, is a comprehensive formulation consisting of proanthocyanidin, biotin, and coenzyme Q10. Probico addresses three primary causes of hair loss: amino acid deficiency, inadequate hair synthesis, and follicle inflammation, excluding the hormonal imbalance and blood circulation issues which require prescription medications.

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