Component

Mitochondrial respiratory complex III

Mitochondrial respiratory complex III. Identity is distinct from its gene and experimentally modified states; see each claim for organism and scope.

5 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. 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

What acts on it

  1. The study identified an ETFDH-complex III-COQ2 assembly directing lipid-derived electrons to the respiratory chain in skeletal muscle.

    Mouse electron transfer flavoprotein dehydrogenase / Etfdh → Mitochondrial respiratory complex III 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
    Fat oxidation and CoQ synthesis connect to the complex that reoxidizes reduced CoQ.
    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 411–422

    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-etfdh-metabolon The study identified an ETFDH-complex III-COQ2 assembly directing lipid-derived electrons to the respiratory chain in skeletal muscle. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Fat oxidation and CoQ synthesis connect to the complex that reoxidizes reduced CoQ. 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. Muscle-specific Etfdh deletion caused complex III dysfunction and myopathy in mice.

    Mouse electron transfer flavoprotein dehydrogenase / Etfdh → Mitochondrial respiratory complex III source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    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
    A defect upstream can disturb the system that recycles the shared electron carrier.
    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
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 437–448

    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-etfdh-muscle-loss Muscle-specific Etfdh deletion caused complex III dysfunction and myopathy in mice. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A defect upstream can disturb the system that recycles the shared electron carrier. 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

Where it participates (unsigned role)

  1. Cardiac Ndufab1 deletion reduced assembled respiratory complexes I–III and supercomplexes in mouse heart mitochondria.

    Mouse mitochondrial acyl carrier protein / Ndufab1 → Mitochondrial respiratory supercomplex assembly source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    true
    evidence_location
    Full text lines 49–55; Fig. 3; Supplementary Figs. S6–S10
    experimental_model
    Cardiomyocyte-specific Ndufab1 knockout mice and isolated heart mitochondria
    exposure
    Cardiac-specific genetic deletion; 6- and 16-week assembly assays, 6- and 10-week respiratory assays.
    limitations
    The FeS subunits of complexes II/III were preferentially affected, whereas broader complex-I subunit loss supports an additional assembly role. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Mus musculus
    plain_language
    Loss of the carrier impaired assembly of several respiratory complexes in mouse heart.
    primary_references
    [b5-met-ndufab2019] NDUFAB1 confers cardio-protection by enhancing mitochondrial bioenergetics through coordination of respiratory complex and supercomplex assembly. (2019). https://pubmed.ncbi.nlm.nih.gov/31366990/ DOI: 10.1038/s41422-019-0208-x
    tissue_or_cell_type
    Heart mitochondria
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 949–961

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cardiomyocyte-specific Ndufab1 knockout mice and isolated heart mitochondria · source_derived_draft · unverified_draft

    ### b5-met-heart-acp-complex-assembly Cardiac Ndufab1 deletion reduced assembled respiratory complexes I–III and supercomplexes in mouse heart mitochondria. Condition category: machinery_impairment nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Loss of the carrier impaired assembly of several respiratory complexes in mouse heart. organism: Mus musculus tissue_or_cell_type: Heart mitochondria experimental_model: Cardiomyocyte-specific Ndufab1 knockout mice and isolated heart mitochondria limitations: The FeS subunits of complexes II/III were preferentially affected, whereas broader complex-I subunit loss supports an additional assembly role. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Cardiac-specific genetic deletion; 6- and 16-week assembly assays, 6- and 10-week respiratory assays. cross_nutrient: true evidence_location: Full text lines 49–55; Fig. 3; Supplementary Figs. S6–S10 [b5-met-ndufab2019] NDUFAB1 confers cardio-protection by enhancing mitochondrial bioenergetics through coordination of respiratory complex and supercomplex assembly. (2019). https://pubmed.ncbi.nlm.nih.gov/31366990/ DOI: 10.1038/s41422-019-0208-x
    Complete structured claim and evidence

  2. Cardiac Ndufab1 deletion lowered oxygen consumption supported by complex I-, II-, or III-linked substrates, while complex IV-linked respiration remained unchanged.

    Mouse mitochondrial acyl carrier protein / Ndufab1 → ADP-stimulated mitochondrial oxygen consumption source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    evidence_location
    Full text lines 47–49; Fig. 3A
    experimental_model
    Cardiomyocyte-specific Ndufab1 knockout mice and isolated heart mitochondria
    exposure
    Cardiac-specific genetic deletion; 6- and 16-week assembly assays, 6- and 10-week respiratory assays.
    limitations
    Isolated-mitochondria oxygen consumption does not measure nutrient absorption or human exercise capacity. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Mus musculus
    plain_language
    The respiratory defect affected several upstream electron-transfer routes but spared the tested complex IV route.
    primary_references
    [b5-met-ndufab2019] NDUFAB1 confers cardio-protection by enhancing mitochondrial bioenergetics through coordination of respiratory complex and supercomplex assembly. (2019). https://pubmed.ncbi.nlm.nih.gov/31366990/ DOI: 10.1038/s41422-019-0208-x
    tissue_or_cell_type
    Heart mitochondria
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 963–975

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cardiomyocyte-specific Ndufab1 knockout mice and isolated heart mitochondria · source_derived_draft · unverified_draft

    ### b5-met-heart-acp-respiration Cardiac Ndufab1 deletion lowered oxygen consumption supported by complex I-, II-, or III-linked substrates, while complex IV-linked respiration remained unchanged. Condition category: machinery_impairment nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: The respiratory defect affected several upstream electron-transfer routes but spared the tested complex IV route. organism: Mus musculus tissue_or_cell_type: Heart mitochondria experimental_model: Cardiomyocyte-specific Ndufab1 knockout mice and isolated heart mitochondria limitations: Isolated-mitochondria oxygen consumption does not measure nutrient absorption or human exercise capacity. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Cardiac-specific genetic deletion; 6- and 16-week assembly assays, 6- and 10-week respiratory assays. cross_nutrient: false evidence_location: Full text lines 47–49; Fig. 3A [b5-met-ndufab2019] NDUFAB1 confers cardio-protection by enhancing mitochondrial bioenergetics through coordination of respiratory complex and supercomplex assembly. (2019). https://pubmed.ncbi.nlm.nih.gov/31366990/ DOI: 10.1038/s41422-019-0208-x
    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