Component

Human mitochondrial manganese superoxide dismutase / SOD2

Human SOD2 protein, distinct from the SOD2 gene and copper-zinc SOD1. Mitochondrial superoxide dismutase / SOD2. Experimental scope belongs to each linked claim.

10 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. Neutron structures of human SOD2 captured Mn(III) and Mn(II) states with coupled changes in active-site protonation.

    Human mitochondrial manganese superoxide dismutase / SOD2 → Mn(III)-bound human SOD2 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Redox-controlled neutron structures of human SOD2
    exposure
    Redox-controlled Mn(III) and Mn(II) crystals
    limitations
    Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens
    plain_language
    SOD2 changes manganese oxidation state as it transfers electrons and protons.
    primary_references
    [mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1
    tissue_or_cell_type
    Purified enzyme; mitochondrial-matrix protein

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 422–432

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Redox-controlled neutron structures of human SOD2 · source_derived_draft · unverified_draft

    ### mn-enz-sod2-redox-states Neutron structures of human SOD2 captured Mn(III) and Mn(II) states with coupled changes in active-site protonation. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: SOD2 changes manganese oxidation state as it transfers electrons and protons. organism: Homo sapiens tissue_or_cell_type: Purified enzyme; mitochondrial-matrix protein experimental_model: Redox-controlled neutron structures of human SOD2 limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Redox-controlled Mn(III) and Mn(II) crystals [mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1
    Complete structured claim and evidence

  2. Human SOD2 uses a Mn(III)/Mn(II) cycle to convert superoxide into oxygen and hydrogen peroxide.

    Human mitochondrial manganese superoxide dismutase / SOD2 → Superoxide dismutation source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Redox-controlled neutron structures of human SOD2
    exposure
    Redox-controlled Mn(III) and Mn(II) crystals
    limitations
    Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens
    plain_language
    SOD2 removes superoxide; it produces hydrogen peroxide that requires further handling.
    primary_references
    [mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1
    tissue_or_cell_type
    Purified enzyme; mitochondrial-matrix protein

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 446–456

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Redox-controlled neutron structures of human SOD2 · source_derived_draft · unverified_draft

    ### mn-enz-sod2-superoxide Human SOD2 uses a Mn(III)/Mn(II) cycle to convert superoxide into oxygen and hydrogen peroxide. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: SOD2 removes superoxide; it produces hydrogen peroxide that requires further handling. organism: Homo sapiens tissue_or_cell_type: Purified enzyme; mitochondrial-matrix protein experimental_model: Redox-controlled neutron structures of human SOD2 limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Redox-controlled Mn(III) and Mn(II) crystals [mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1
    Complete structured claim and evidence

  3. Increasing yeast growth temperature increased both manganese content and activity of mitochondrially expressed human SOD2.

    Human mitochondrial manganese superoxide dismutase / SOD2 → Human SOD2 metallation source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria
    exposure
    Heterologous expression; metallation and reconstitution
    limitations
    Human protein in yeast; this finding is not a recommendation to alter human body temperature.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Human protein in Saccharomyces cerevisiae
    plain_language
    SOD2 metal loading depended on the experimental expression conditions.
    primary_references
    [mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016
    tissue_or_cell_type
    Yeast mitochondria

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 483–493

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria · source_derived_draft · unverified_draft

    ### mn-enz-sod2-yeast-temperature Increasing yeast growth temperature increased both manganese content and activity of mitochondrially expressed human SOD2. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: SOD2 metal loading depended on the experimental expression conditions. organism: Human protein in Saccharomyces cerevisiae tissue_or_cell_type: Yeast mitochondria experimental_model: Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria limitations: Human protein in yeast; this finding is not a recommendation to alter human body temperature. exposure: Heterologous expression; metallation and reconstitution [mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016
    Complete structured claim and evidence

What acts on it

  1. Mangiferin opposed H2O2-associated loss of manganese superoxide dismutase expression and activity.

    Mangiferin → Human mitochondrial manganese superoxide dismutase / SOD2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/38586992.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be", "start_char": 0, "end_char": 1792, "text_sha256": "3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be"}
    experimental_model
    Hydrogen-peroxide challenge with pharmacological HO-1 inhibition
    exposure
    Mangiferin before H2O2 exposure
    limitations
    Cell protection is not demonstrated retinal clinical efficacy; GPx isoforms unresolved and expression is not cofactor sufficiency.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Homo sapiens
    plain_language
    An enzyme that depends on manganese was part of the measured response.
    primary_references
    [mangiferin-p38586992] Activation of Heme Oxygenase-1 by Mangiferin in Human Retinal Pigment Epithelial Cells Contributes to Blocking Oxidative Damage. (2024). https://pubmed.ncbi.nlm.nih.gov/38586992/ DOI: 10.4062/biomolther.2023.175
    tissue_or_cell_type
    ARPE-19 retinal pigment epithelial cells

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 614–625

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hydrogen-peroxide challenge with pharmacological HO-1 inhibition · source_derived_draft · unverified_draft

    ### mangiferin-rpe-sod2 Mangiferin opposed H2O2-associated loss of manganese superoxide dismutase expression and activity. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: An enzyme that depends on manganese was part of the measured response. organism: Homo sapiens tissue_or_cell_type: ARPE-19 retinal pigment epithelial cells experimental_model: Hydrogen-peroxide challenge with pharmacological HO-1 inhibition limitations: Cell protection is not demonstrated retinal clinical efficacy; GPx isoforms unresolved and expression is not cofactor sufficiency. exposure: Mangiferin before H2O2 exposure evidence_span: {"source_cache": "artifacts/mangiferin-research/38586992.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be", "start_char": 0, "end_char": 1792, "text_sha256": "3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be"} [mangiferin-p38586992] Activation of Heme Oxygenase-1 by Mangiferin in Human Retinal Pigment Epithelial Cells Contributes to Blocking Oxidative Damage. (2024). https://pubmed.ncbi.nlm.nih.gov/38586992/ DOI: 10.4062/biomolther.2023.175
    Complete structured claim and evidence

  2. The authors suggest that release of free iron from the degradation of heme by heme oxygenase-1 may have played a role in the later upregulation of the manganese dismutase.

    Human heme oxygenase 1 / HMOX1 → Human mitochondrial manganese superoxide dismutase / SOD2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"}
    experimental_model
    Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR
    exposure
    99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days
    limitations
    Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Human cells
    plain_language
    Iron freed from heme may be the signal that calls up the manganese enzyme.
    primary_references
    [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    tissue_or_cell_type
    Lens epithelium

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 439–450

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR · source_derived_draft · unverified_draft

    ### hbot-ho1-iron-to-mnsod The authors suggest that release of free iron from the degradation of heme by heme oxygenase-1 may have played a role in the later upregulation of the manganese dismutase. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: Iron freed from heme may be the signal that calls up the manganese enzyme. organism: Human cells tissue_or_cell_type: Lens epithelium experimental_model: Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR limitations: Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant. exposure: 99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days evidence_span: {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"} [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    Complete structured claim and evidence

  3. The human SOD2 active-site manganese is coordinated by His26, His74, His163, Asp159 and a water/hydroxide ligand in the structural model.

    Mn2+ → Human mitochondrial manganese superoxide dismutase / SOD2 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Redox-controlled neutron structures of human SOD2
    exposure
    Redox-controlled Mn(III) and Mn(II) crystals
    limitations
    Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens
    plain_language
    A defined protein pocket holds manganese for SOD2 chemistry.
    primary_references
    [mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1
    tissue_or_cell_type
    Purified enzyme; mitochondrial-matrix protein

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 434–444

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Redox-controlled neutron structures of human SOD2 · source_derived_draft · unverified_draft

    ### mn-enz-sod2-coordination The human SOD2 active-site manganese is coordinated by His26, His74, His163, Asp159 and a water/hydroxide ligand in the structural model. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: A defined protein pocket holds manganese for SOD2 chemistry. organism: Homo sapiens tissue_or_cell_type: Purified enzyme; mitochondrial-matrix protein experimental_model: Redox-controlled neutron structures of human SOD2 limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Redox-controlled Mn(III) and Mn(II) crystals [mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Messenger RNA for heme oxygenase-1, manganese superoxide dismutase and cytoplasmic thioredoxin reductase 1 rose three- to six-fold nine hours after exposure, with heme oxygenase-1 rising a few hours before manganese superoxide dismutase, while catalase, copper-zinc superoxide dismutase, glutathione reductase, glutathione peroxidase and thioredoxin did not change.

    Hyperbaric oxygen therapy → TXNRD1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"}
    experimental_model
    Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR
    exposure
    99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days
    limitations
    Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Human cells
    plain_language
    The cell rebuilt exactly three proteins: the heme enzyme, the manganese enzyme and the selenium enzyme.
    primary_references
    [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    tissue_or_cell_type
    Lens epithelium

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 426–437

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR · source_derived_draft · unverified_draft

    ### hbot-trxr-mrna-response Messenger RNA for heme oxygenase-1, manganese superoxide dismutase and cytoplasmic thioredoxin reductase 1 rose three- to six-fold nine hours after exposure, with heme oxygenase-1 rising a few hours before manganese superoxide dismutase, while catalase, copper-zinc superoxide dismutase, glutathione reductase, glutathione peroxidase and thioredoxin did not change. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The cell rebuilt exactly three proteins: the heme enzyme, the manganese enzyme and the selenium enzyme. organism: Human cells tissue_or_cell_type: Lens epithelium experimental_model: Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR limitations: Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant. exposure: 99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days evidence_span: {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"} [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    Complete structured claim and evidence

  2. Manganese supplementation increased lymphocyte MnSOD activity from baseline.

    Manganese → Lymphocyte manganese superoxide dismutase activity source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Mitochondrial superoxide dismutase / SOD2 (measured_enzyme); Iron (factorial_comparator)
    evidence_span
    {"source_cache": "artifacts/manganese-clinical-sources/davis1992a.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "2fbf15cf32ba80f68c4f4efaa7fa50de76b90094438325cc6632b7d447e22227", "start_char": 0, "end_char": 956, "text_sha256": "2fbf15cf32ba80f68c4f4efaa7fa50de76b90094438325cc6632b7d447e22227", "text_characters": 956}
    experimental_model
    124-day supplementation study in 47 women
    exposure
    Placebo, 60 mg iron/day, 15 mg manganese/day or both.
    limitations
    Historical experimental doses, not intake advice. Abstract reports manganese changes from baseline; biomarkers do not demonstrate improved health or establish a deficiency threshold.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens
    plain_language
    The manganese enzyme responded in the sampled immune cells.
    primary_references
    [mn-clin-davis1992a] Longitudinal changes of manganese-dependent superoxide dismutase and other indexes of manganese and iron status in women. (1992). https://pubmed.ncbi.nlm.nih.gov/1550052/ DOI: 10.1093/ajcn/55.3.747
    tissue_or_cell_type
    Lymphocytes, serum and urine

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 1104–1116

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · 124-day supplementation study in 47 women · source_derived_draft · unverified_draft

    ### mn-clin-supplement-lymphocyte-sod Manganese supplementation increased lymphocyte MnSOD activity from baseline. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: The manganese enzyme responded in the sampled immune cells. organism: Homo sapiens tissue_or_cell_type: Lymphocytes, serum and urine experimental_model: 124-day supplementation study in 47 women limitations: Historical experimental doses, not intake advice. Abstract reports manganese changes from baseline; biomarkers do not demonstrate improved health or establish a deficiency threshold. exposure: Placebo, 60 mg iron/day, 15 mg manganese/day or both. cross_nutrient: Mitochondrial superoxide dismutase / SOD2 (measured_enzyme); Iron (factorial_comparator) evidence_span: {"source_cache": "artifacts/manganese-clinical-sources/davis1992a.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "2fbf15cf32ba80f68c4f4efaa7fa50de76b90094438325cc6632b7d447e22227", "start_char": 0, "end_char": 956, "text_sha256": "2fbf15cf32ba80f68c4f4efaa7fa50de76b90094438325cc6632b7d447e22227", "text_characters": 956} [mn-clin-davis1992a] Longitudinal changes of manganese-dependent superoxide dismutase and other indexes of manganese and iron status in women. (1992). https://pubmed.ncbi.nlm.nih.gov/1550052/ DOI: 10.1093/ajcn/55.3.747
    Complete structured claim and evidence

  3. Human SOD1 maturation involves copper and zinc insertion and a Cys57–Cys146 disulfide; this is a different metalloprotein system from manganese SOD2.

    Human copper-zinc superoxide dismutase / SOD1 → SOD1 maturation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Copper and zinc cofactor identity in SOD1 is distinguished from Mn-dependent SOD2.
    experimental_model
    NMR of copper-depleted human SOD1 C6A/C111S preparation
    exposure
    Copper-depleted zinc-containing disulfide-reduced preparation
    limitations
    The study structurally examined the C6A/C111S copper-depleted, zinc-containing preparation. This identity statement does not assert Mn can replace either SOD1 metal.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens protein
    plain_language
    SOD1 and SOD2 use different metals.
    primary_references
    [mn-enz-16291742] Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. (2006). https://pubmed.ncbi.nlm.nih.gov/16291742/ DOI: 10.1074/jbc.m506497200
    tissue_or_cell_type
    Purified SOD1

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 458–469

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · NMR of copper-depleted human SOD1 C6A/C111S preparation · source_derived_draft · unverified_draft

    ### mn-enz-sod1-distinct-metals Human SOD1 maturation involves copper and zinc insertion and a Cys57–Cys146 disulfide; this is a different metalloprotein system from manganese SOD2. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: SOD1 and SOD2 use different metals. organism: Homo sapiens protein tissue_or_cell_type: Purified SOD1 experimental_model: NMR of copper-depleted human SOD1 C6A/C111S preparation limitations: The study structurally examined the C6A/C111S copper-depleted, zinc-containing preparation. This identity statement does not assert Mn can replace either SOD1 metal. exposure: Copper-depleted zinc-containing disulfide-reduced preparation cross_nutrient: Copper and zinc cofactor identity in SOD1 is distinguished from Mn-dependent SOD2. [mn-enz-16291742] Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. (2006). https://pubmed.ncbi.nlm.nih.gov/16291742/ DOI: 10.1074/jbc.m506497200
    Complete structured claim and evidence

  4. At 30 °C, more than half of human SOD2 purified from expressing yeast mitochondria was apoprotein, and that apoprotein could be fully activated by reconstitution.

    Metal-free human SOD2 → Human SOD2 metallation source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria
    exposure
    Heterologous expression; metallation and reconstitution
    limitations
    Heterologous yeast expression, not endogenous human tissue. The indexed abstract does not specify a reconstitution dose.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Human protein in Saccharomyces cerevisiae
    plain_language
    Making SOD2 protein does not guarantee that it has loaded its metal.
    primary_references
    [mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016
    tissue_or_cell_type
    Yeast mitochondria

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 471–481

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria · source_derived_draft · unverified_draft

    ### mn-enz-sod2-yeast-apo At 30 °C, more than half of human SOD2 purified from expressing yeast mitochondria was apoprotein, and that apoprotein could be fully activated by reconstitution. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Making SOD2 protein does not guarantee that it has loaded its metal. organism: Human protein in Saccharomyces cerevisiae tissue_or_cell_type: Yeast mitochondria experimental_model: Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria limitations: Heterologous yeast expression, not endogenous human tissue. The indexed abstract does not specify a reconstitution dose. exposure: Heterologous expression; metallation and reconstitution [mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016
    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