Component

Ubiquinone-10

Oxidized coenzyme Q10 with ten isoprenoid units; more specific than the canonical generic ubiquinone.

12 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. Ubiquinone-10 had the highest binding affinity and fastest binding rate among the tested chain lengths; ubiquinol-10 release was not rate limiting.

    Ubiquinone-10 → Mitochondrial respiratory complex I source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"}
    experimental_model
    Proteoliposome enzyme kinetics
    exposure
    Ubiquinones with one to ten isoprenoid units
    limitations
    Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Mammalian complex I preparation
    plain_language
    The ten-unit tail is part of the working molecule, not an inert label.
    primary_references
    [coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
    tissue_or_cell_type
    Membrane quinone channel

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 398–409

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Proteoliposome enzyme kinetics · source_derived_draft · unverified_draft

    ### coq10-complex-i-tail Ubiquinone-10 had the highest binding affinity and fastest binding rate among the tested chain lengths; ubiquinol-10 release was not rate limiting. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The ten-unit tail is part of the working molecule, not an inert label. organism: Mammalian complex I preparation tissue_or_cell_type: Membrane quinone channel experimental_model: Proteoliposome enzyme kinetics limitations: Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10. exposure: Ubiquinones with one to ten isoprenoid units evidence_span: {"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"} [coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
    Complete structured claim and evidence

  2. CoQ appeared in blood predominantly as ubiquinol regardless of which of the tested redox forms was consumed.

    Ubiquinone-10 → Reduced CoQ10 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"}
    experimental_model
    Randomized three-period crossover pharmacokinetic study
    exposure
    Single equivalent 100-mg doses in three formulations
    limitations
    Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    21 healthy adults aged 65-74
    plain_language
    The form swallowed and the form circulating are not necessarily the same.
    primary_references
    [coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
    tissue_or_cell_type
    Plasma total CoQ and redox state over 48 hours

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 892–903

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized three-period crossover pharmacokinetic study · source_derived_draft · unverified_draft

    ### coq10-oral-redox CoQ appeared in blood predominantly as ubiquinol regardless of which of the tested redox forms was consumed. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The form swallowed and the form circulating are not necessarily the same. organism: 21 healthy adults aged 65-74 tissue_or_cell_type: Plasma total CoQ and redox state over 48 hours experimental_model: Randomized three-period crossover pharmacokinetic study limitations: Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product. exposure: Single equivalent 100-mg doses in three formulations evidence_span: {"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"} [coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
    Complete structured claim and evidence

  3. The same solution study detected no reaction of oxidized ubiquinone-10 with tocopheroxyl radicals, distinguishing it from the active reduced ubiquinol-10 form.

    Ubiquinone-10 → Alpha-tocopherol source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    Primary abstract
    experimental_model
    Stopped-flow comparison of CoQ10 redox states
    exposure
    Oxidized ubiquinone-10 comparator.
    limitations
    A non-detected reaction under these assay conditions is not an assertion that cellular CoQ cannot first be reduced.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Cell-free
    plain_language
    CoQ10 needed to be in its reduced state for the measured recycling reaction.
    primary_references
    [ver-mukai1990] Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution. (1990). https://pubmed.ncbi.nlm.nih.gov/2383582/ DOI: 10.1016/0304-4165(90)90176-w
    tissue_or_cell_type
    Chemical solution

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 522–534

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stopped-flow comparison of CoQ10 redox states · source_derived_draft · unverified_draft

    ### ver-oxidized-coq-no-regeneration The same solution study detected no reaction of oxidized ubiquinone-10 with tocopheroxyl radicals, distinguishing it from the active reduced ubiquinol-10 form. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ10 needed to be in its reduced state for the measured recycling reaction. organism: Cell-free tissue_or_cell_type: Chemical solution experimental_model: Stopped-flow comparison of CoQ10 redox states limitations: A non-detected reaction under these assay conditions is not an assertion that cellular CoQ cannot first be reduced. exposure: Oxidized ubiquinone-10 comparator. cross_nutrient: true evidence_location: Primary abstract [ver-mukai1990] Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution. (1990). https://pubmed.ncbi.nlm.nih.gov/2383582/ DOI: 10.1016/0304-4165(90)90176-w
    Complete structured claim and evidence

What acts on it

  1. Complex I transferred electrons from NADH to ubiquinone-10 in reconstituted membranes.

    Mitochondrial respiratory complex I → Ubiquinone-10 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"}
    experimental_model
    Proteoliposome enzyme kinetics
    exposure
    Ubiquinones with one to ten isoprenoid units
    limitations
    Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Mammalian complex I preparation
    plain_language
    CoQ receives electrons from the first respiratory complex.
    primary_references
    [coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
    tissue_or_cell_type
    Membrane quinone channel

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 385–396

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Proteoliposome enzyme kinetics · source_derived_draft · unverified_draft

    ### coq10-complex-i-q Complex I transferred electrons from NADH to ubiquinone-10 in reconstituted membranes. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ receives electrons from the first respiratory complex. organism: Mammalian complex I preparation tissue_or_cell_type: Membrane quinone channel experimental_model: Proteoliposome enzyme kinetics limitations: Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10. exposure: Ubiquinones with one to ten isoprenoid units evidence_span: {"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"} [coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
    Complete structured claim and evidence

  2. Truncated human DHODH penetrated the outer lipid leaflet toward membrane-embedded Q10.

    Human dihydroorotate dehydrogenase / DHODH → Ubiquinone-10 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/35269583.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a", "start_char": 0, "end_char": 1389, "text_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a"}
    experimental_model
    Neutron reflectometry in supported lipid membranes
    exposure
    Membrane composition and Q10 placement
    limitations
    Truncated human enzyme and synthetic bilayers, not complete mitochondrial nucleotide flux.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Truncated human DHODH and E. coli DHODH
    plain_language
    The enzyme that helps make pyrimidines must reach its electron acceptor in the membrane.
    primary_references
    [coq10-p35269583] New Insights into the Interaction of Class II Dihydroorotate Dehydrogenases with Ubiquinone in Lipid Bilayers as a Function of Lipid Composition. (2022). https://pubmed.ncbi.nlm.nih.gov/35269583/ DOI: 10.3390/ijms23052437
    tissue_or_cell_type
    Ubiquinone-containing bilayers

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 450–461

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Neutron reflectometry in supported lipid membranes · source_derived_draft · unverified_draft

    ### coq10-dhodh-q-access Truncated human DHODH penetrated the outer lipid leaflet toward membrane-embedded Q10. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme that helps make pyrimidines must reach its electron acceptor in the membrane. organism: Truncated human DHODH and E. coli DHODH tissue_or_cell_type: Ubiquinone-containing bilayers experimental_model: Neutron reflectometry in supported lipid membranes limitations: Truncated human enzyme and synthetic bilayers, not complete mitochondrial nucleotide flux. exposure: Membrane composition and Q10 placement evidence_span: {"source_cache": "artifacts/coq10-research/35269583.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a", "start_char": 0, "end_char": 1389, "text_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a"} [coq10-p35269583] New Insights into the Interaction of Class II Dihydroorotate Dehydrogenases with Ubiquinone in Lipid Bilayers as a Function of Lipid Composition. (2022). https://pubmed.ncbi.nlm.nih.gov/35269583/ DOI: 10.3390/ijms23052437
    Complete structured claim and evidence

  3. Comparison with selenium-deprived and truncated mammalian TrxR forms showed selenium-dependent ubiquinone reduction.

    TXNRD1 → Ubiquinone-10 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"}
    experimental_model
    Enzyme kinetics, mutants and overexpressing-cell homogenates
    exposure
    NADPH or NADH; selenite and selenium-deprived enzyme variants
    limitations
    Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Mammalian TrxR1 and human HEK293 cells
    plain_language
    The chemistry depends on the enzyme being assembled correctly.
    primary_references
    [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
    tissue_or_cell_type
    Ubiquinone reduction
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 775–786

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft

    ### coq10-txnrd-selenium Comparison with selenium-deprived and truncated mammalian TrxR forms showed selenium-dependent ubiquinone reduction. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The chemistry depends on the enzyme being assembled correctly. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically. exposure: NADPH or NADH; selenite and selenium-deprived enzyme variants evidence_span: {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"} [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
    Complete structured claim and evidence

  4. Mammalian TrxR1 reduced ubiquinone-10 to ubiquinol-10.

    TXNRD1 → Ubiquinone-10 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"}
    experimental_model
    Enzyme kinetics, mutants and overexpressing-cell homogenates
    exposure
    NADPH or NADH; selenite and selenium-deprived enzyme variants
    limitations
    Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Mammalian TrxR1 and human HEK293 cells
    plain_language
    A selenium-dependent enzyme can regenerate the antioxidant form of CoQ.
    primary_references
    [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
    tissue_or_cell_type
    Ubiquinone reduction

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 762–773

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft

    ### coq10-txnrd1-coq Mammalian TrxR1 reduced ubiquinone-10 to ubiquinol-10. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A selenium-dependent enzyme can regenerate the antioxidant form of CoQ. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically. exposure: NADPH or NADH; selenite and selenium-deprived enzyme variants evidence_span: {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"} [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Complex III oxidizes reduced CoQ as part of respiratory electron flow examined in this study.

    Mitochondrial respiratory complex III → Reduced CoQ10 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/38243131.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de9afaeca8a144d79c9f0d0d3b3faafaa4560af2292b8624d1a04ed45ee5d136", "start_char": 0, "end_char": 1039, "text_sha256": "de9afaeca8a144d79c9f0d0d3b3faafaa4560af2292b8624d1a04ed45ee5d136"}
    experimental_model
    Muscle-specific knockout and protein-complex analyses
    exposure
    Etfdh deletion and metabolon characterization
    limitations
    Skeletal-muscle context; does not establish identical complex organization in every human tissue.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Mouse skeletal muscle and biochemical systems
    plain_language
    The carrier must release its electrons before it can accept more.
    primary_references
    [coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
    tissue_or_cell_type
    ETFDH-complex III-COQ2 assembly

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 424–435

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Muscle-specific knockout and protein-complex analyses · source_derived_draft · unverified_draft

    ### coq10-complex-iii-q Complex III oxidizes reduced CoQ as part of respiratory electron flow examined in this study. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The carrier must release its electrons before it can accept more. organism: Mouse skeletal muscle and biochemical systems tissue_or_cell_type: ETFDH-complex III-COQ2 assembly experimental_model: Muscle-specific knockout and protein-complex analyses limitations: Skeletal-muscle context; does not establish identical complex organization in every human tissue. exposure: Etfdh deletion and metabolon characterization evidence_span: {"source_cache": "artifacts/coq10-research/38243131.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de9afaeca8a144d79c9f0d0d3b3faafaa4560af2292b8624d1a04ed45ee5d136", "start_char": 0, "end_char": 1039, "text_sha256": "de9afaeca8a144d79c9f0d0d3b3faafaa4560af2292b8624d1a04ed45ee5d136"} [coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
    Complete structured claim and evidence

  2. The tested water-soluble formulation had 2.4-fold higher baseline-corrected exposure than standard ubiquinone capsules; the ubiquinol-capsule comparison was not statistically significant.

    Coenzyme Q10 / CoQ10 redox system → Plasma coenzyme Q10 concentration source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"}
    experimental_model
    Randomized three-period crossover pharmacokinetic study
    exposure
    Single equivalent 100-mg doses in three formulations
    limitations
    Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    21 healthy adults aged 65-74
    plain_language
    The formulation mattered; the redox-form label alone did not establish superiority.
    primary_references
    [coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
    tissue_or_cell_type
    Plasma total CoQ and redox state over 48 hours

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 879–890

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized three-period crossover pharmacokinetic study · source_derived_draft · unverified_draft

    ### coq10-formulation-exposure The tested water-soluble formulation had 2.4-fold higher baseline-corrected exposure than standard ubiquinone capsules; the ubiquinol-capsule comparison was not statistically significant. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The formulation mattered; the redox-form label alone did not establish superiority. organism: 21 healthy adults aged 65-74 tissue_or_cell_type: Plasma total CoQ and redox state over 48 hours experimental_model: Randomized three-period crossover pharmacokinetic study limitations: Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product. exposure: Single equivalent 100-mg doses in three formulations evidence_span: {"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"} [coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
    Complete structured claim and evidence

  3. Selenite treatment increased cytosolic TrxR activity together with ubiquinone reduction in the tested cell homogenates.

    Selenite ion → TrxR1-associated ubiquinone reductase activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"}
    experimental_model
    Enzyme kinetics, mutants and overexpressing-cell homogenates
    exposure
    NADPH or NADH; selenite and selenium-deprived enzyme variants
    limitations
    Cell-culture exposure; no clinical supplement ratio or systemic outcome was tested.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Mammalian TrxR1 and human HEK293 cells
    plain_language
    A cell experiment connected selenium supply with CoQ recycling capacity.
    primary_references
    [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
    tissue_or_cell_type
    Ubiquinone reduction

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 788–799

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft

    ### coq10-selenite-cell-recycling Selenite treatment increased cytosolic TrxR activity together with ubiquinone reduction in the tested cell homogenates. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A cell experiment connected selenium supply with CoQ recycling capacity. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Cell-culture exposure; no clinical supplement ratio or systemic outcome was tested. exposure: NADPH or NADH; selenite and selenium-deprived enzyme variants evidence_span: {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"} [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
    Complete structured claim and evidence

  4. Vitamin K2 entered mitochondria but restored neither respiratory electron flow nor ATP synthesis in CoQ-deficient human cells and yeast; CoQ4 did restore function.

    Menaquinone-4 / MK-4 / menatetrenone → Mitochondrial respiratory electron transfer source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/k2-research/31024065.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e", "start_char": 0, "end_char": 943, "text_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e"}
    experimental_model
    Cellular uptake and respiratory rescue comparisons
    exposure
    MK-4 versus CoQ4
    limitations
    Different organism and deficiency model from the fly study; failure here is a boundary to extrapolation, not a clerical error in either experiment.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Human CoQ10-deficient cell lines and CoQ6-deficient yeast
    plain_language
    Getting into the organelle did not make MK-4 a functional substitute for CoQ.
    primary_references
    [k2-p31024065] Vitamin K2 cannot substitute Coenzyme Q10 as electron carrier in the mitochondrial respiratory chain of mammalian cells. (2019). https://pubmed.ncbi.nlm.nih.gov/31024065/ DOI: 10.1038/s41598-019-43014-y
    tissue_or_cell_type
    Mitochondrial respiratory chain
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 877–888

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cellular uptake and respiratory rescue comparisons · source_derived_draft · unverified_draft

    ### k2-mk4-not-coq Vitamin K2 entered mitochondria but restored neither respiratory electron flow nor ATP synthesis in CoQ-deficient human cells and yeast; CoQ4 did restore function. Condition category: machinery_impairment nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Getting into the organelle did not make MK-4 a functional substitute for CoQ. organism: Human CoQ10-deficient cell lines and CoQ6-deficient yeast tissue_or_cell_type: Mitochondrial respiratory chain experimental_model: Cellular uptake and respiratory rescue comparisons limitations: Different organism and deficiency model from the fly study; failure here is a boundary to extrapolation, not a clerical error in either experiment. exposure: MK-4 versus CoQ4 evidence_span: {"source_cache": "artifacts/k2-research/31024065.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e", "start_char": 0, "end_char": 943, "text_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e"} [k2-p31024065] Vitamin K2 cannot substitute Coenzyme Q10 as electron carrier in the mitochondrial respiratory chain of mammalian cells. (2019). https://pubmed.ncbi.nlm.nih.gov/31024065/ DOI: 10.1038/s41598-019-43014-y
    Complete structured claim and evidence

  5. Berberine inhibited respiration in L6 myotubes and muscle mitochondria through a complex-I-associated effect.

    Berberine → Mitochondrial respiratory complex I source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/berberine-research/18285556.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cd721d78117d554be4fdb0403ac792f6723cf59cfd3679106607e8f17eafc257", "start_char": 0, "end_char": 1735, "text_sha256": "cd721d78117d554be4fdb0403ac792f6723cf59cfd3679106607e8f17eafc257"}
    experimental_model
    Cell respiration, isolated mitochondria and kinase perturbation
    exposure
    Berberine concentration-response; kinase deletion/inhibition
    limitations
    Functional respiratory inhibition does not by itself establish direct binding to complex I or improved mitochondrial health. Preclinical exposure, not human efficacy.
    nutrient_topic
    Berberine research collection; topical membership is not evidence of a direct dietary effect. · Berberine
    organism
    Rat L6 myotubes, muscle mitochondria and LKB1-deficient cells
    plain_language
    Slowing one respiratory-chain step can trigger a cellular energy response.
    primary_references
    [berberine-p18285556] Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: a mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action. (2008). https://pubmed.ncbi.nlm.nih.gov/18285556/ DOI: 10.2337/db07-1552
    tissue_or_cell_type
    Respiratory complex I and AMPK

    Berberine: metabolism, nutrient connections and drug interactions (2026-09-17) · lines 324–335

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell respiration, isolated mitochondria and kinase perturbation · source_derived_draft · unverified_draft

    ### berberine-complex-i Berberine inhibited respiration in L6 myotubes and muscle mitochondria through a complex-I-associated effect. Condition category: normal nutrient_topic: Berberine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Slowing one respiratory-chain step can trigger a cellular energy response. organism: Rat L6 myotubes, muscle mitochondria and LKB1-deficient cells tissue_or_cell_type: Respiratory complex I and AMPK experimental_model: Cell respiration, isolated mitochondria and kinase perturbation limitations: Functional respiratory inhibition does not by itself establish direct binding to complex I or improved mitochondrial health. Preclinical exposure, not human efficacy. exposure: Berberine concentration-response; kinase deletion/inhibition evidence_span: {"source_cache": "artifacts/berberine-research/18285556.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cd721d78117d554be4fdb0403ac792f6723cf59cfd3679106607e8f17eafc257", "start_char": 0, "end_char": 1735, "text_sha256": "cd721d78117d554be4fdb0403ac792f6723cf59cfd3679106607e8f17eafc257"} [berberine-p18285556] Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: a mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action. (2008). https://pubmed.ncbi.nlm.nih.gov/18285556/ DOI: 10.2337/db07-1552
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards