Component

Mitochondrial respiratory electron transfer

Mitochondrial respiratory electron transfer. Species, exposure and limitations are retained in each linked claim.

4 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 acts on it

  1. Adding quinone restored CoQ-dependent respiratory activities in the tested deficient preparations.

    Ubiquinone → Mitochondrial respiratory electron transfer source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/17332895.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87", "start_char": 0, "end_char": 1416, "text_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87"}
    experimental_model
    Pedigrees, respiratory assays and yeast complementation
    exposure
    PDSS1 D308E or COQ2 frameshift variants
    limitations
    Distinct families and mutations; quinone rescue in an assay is not equivalent to proven oral treatment of every organ.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Human families and yeast validation
    plain_language
    An intact respiratory enzyme can still fail when its mobile electron carrier is missing.
    primary_references
    [coq10-p17332895] Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. (2007). https://pubmed.ncbi.nlm.nih.gov/17332895/ DOI: 10.1172/jci29089
    tissue_or_cell_type
    CoQ-dependent respiratory function

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 216–227

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pedigrees, respiratory assays and yeast complementation · source_derived_draft · unverified_draft

    ### coq10-quinone-rescue-assay Adding quinone restored CoQ-dependent respiratory activities in the tested deficient preparations. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: An intact respiratory enzyme can still fail when its mobile electron carrier is missing. organism: Human families and yeast validation tissue_or_cell_type: CoQ-dependent respiratory function experimental_model: Pedigrees, respiratory assays and yeast complementation limitations: Distinct families and mutations; quinone rescue in an assay is not equivalent to proven oral treatment of every organ. exposure: PDSS1 D308E or COQ2 frameshift variants evidence_span: {"source_cache": "artifacts/coq10-research/17332895.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87", "start_char": 0, "end_char": 1416, "text_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87"} [coq10-p17332895] Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. (2007). https://pubmed.ncbi.nlm.nih.gov/17332895/ DOI: 10.1172/jci29089
    Complete structured claim and evidence

  2. Respiratory-chain enzyme and citrate-synthase activities were lower in the selected simvastatin subgroup with marked muscle CoQ decline.

    Simvastatin → 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/coq10-research/16003294.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b", "start_char": 0, "end_char": 1774, "text_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b"}
    experimental_model
    Randomized double-blind placebo-controlled trial with muscle biopsies
    exposure
    Simvastatin 80 mg/day, atorvastatin 40 mg/day or placebo for eight weeks
    limitations
    Six selected simvastatin participants were compared with matched participants from other arms. Selection and mitochondrial-content changes prevent assigning the entire effect specifically to CoQ depletion.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    48 hypercholesterolemic adults in three groups
    plain_language
    Both respiratory capacity and a mitochondrial-content marker changed in a selected subgroup.
    primary_references
    [coq10-p16003294] High-dose statins and skeletal muscle metabolism in humans: a randomized, controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/16003294/ DOI: 10.1016/j.clpt.2005.03.006
    tissue_or_cell_type
    Muscle CoQ and respiratory enzymes
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 970–981

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial with muscle biopsies · source_derived_draft · unverified_draft

    ### coq10-statin-respiratory-subset Respiratory-chain enzyme and citrate-synthase activities were lower in the selected simvastatin subgroup with marked muscle CoQ decline. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Both respiratory capacity and a mitochondrial-content marker changed in a selected subgroup. organism: 48 hypercholesterolemic adults in three groups tissue_or_cell_type: Muscle CoQ and respiratory enzymes experimental_model: Randomized double-blind placebo-controlled trial with muscle biopsies limitations: Six selected simvastatin participants were compared with matched participants from other arms. Selection and mitochondrial-content changes prevent assigning the entire effect specifically to CoQ depletion. exposure: Simvastatin 80 mg/day, atorvastatin 40 mg/day or placebo for eight weeks evidence_span: {"source_cache": "artifacts/coq10-research/16003294.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b", "start_char": 0, "end_char": 1774, "text_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b"} [coq10-p16003294] High-dose statins and skeletal muscle metabolism in humans: a randomized, controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/16003294/ DOI: 10.1016/j.clpt.2005.03.006
    Complete structured claim and evidence

  3. Vitamin K2 transferred electrons in Drosophila mitochondria and improved ATP production; Heix-mutant defects were rescued by K2.

    Vitamin K2 / menaquinone family → 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/22582012.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1f7c8600fd883b912c1fd697b1bffb6e442e2763230347e5c198d88c0c6bb4cc", "start_char": 0, "end_char": 926, "text_sha256": "1f7c8600fd883b912c1fd697b1bffb6e442e2763230347e5c198d88c0c6bb4cc"}
    experimental_model
    Genetic modifier and mitochondrial function experiments
    exposure
    Heix/Pink1 defects and vitamin K2 rescue
    limitations
    Fly electron-transfer rescue does not establish replacement of human CoQ10 or treatment of Parkinson disease.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Drosophila
    plain_language
    An energy role was found in flies and is recorded with that species boundary.
    primary_references
    [k2-p22582012] Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency. (2012). https://pubmed.ncbi.nlm.nih.gov/22582012/ DOI: 10.1126/science.1218632
    tissue_or_cell_type
    Mitochondria
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 864–875

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genetic modifier and mitochondrial function experiments · source_derived_draft · unverified_draft

    ### k2-fly-mitochondria Vitamin K2 transferred electrons in Drosophila mitochondria and improved ATP production; Heix-mutant defects were rescued by K2. Condition category: machinery_impairment nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: An energy role was found in flies and is recorded with that species boundary. organism: Drosophila tissue_or_cell_type: Mitochondria experimental_model: Genetic modifier and mitochondrial function experiments limitations: Fly electron-transfer rescue does not establish replacement of human CoQ10 or treatment of Parkinson disease. exposure: Heix/Pink1 defects and vitamin K2 rescue evidence_span: {"source_cache": "artifacts/k2-research/22582012.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1f7c8600fd883b912c1fd697b1bffb6e442e2763230347e5c198d88c0c6bb4cc", "start_char": 0, "end_char": 926, "text_sha256": "1f7c8600fd883b912c1fd697b1bffb6e442e2763230347e5c198d88c0c6bb4cc"} [k2-p22582012] Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency. (2012). https://pubmed.ncbi.nlm.nih.gov/22582012/ DOI: 10.1126/science.1218632
    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

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.

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