sulfur globule

traitmech:000069 · CLASS · REVIEWED

An intracellular (or periplasmic) inclusion of elemental sulfur formed as an intermediate during the oxidation of reduced sulfur compounds, characteristic of many sulfur-oxidizing and phototrophic sulfur bacteria.

Sulfur globules store elemental sulfur during oxidative sulfur metabolism

Evidence-backed causal sketch linking oxidative sulfur metabolism to deposition of elemental sulfur as intracellular/periplasmic globules.

Sulfur globules store elemental sulfur during oxidative sulfur metabolism Interactive directed graph showing evidence-backed causal relationships for sulfur globule.

Edge evidence

  • oxidative sulfur metabolism produces elemental sulfur METPO:2000202

    Oxidation of reduced sulfur compounds generates elemental sulfur as an intermediate.

    • DOI:10.1016/S0065-2911(08)00002-7 Frigaard & Dahl describe sulfur globules as sulfur-storage intermediates formed during oxidative sulfur metabolism.
  • elemental sulfur located in sulfur globule biolink:located_in

    The deposited elemental sulfur forms a globule inclusion.

    • DOI:10.1038/s41579-020-0413-0 Greening & Lithgow include sulfur globules among bacterial intracellular storage inclusions.
  • sulfide:quinone oxidoreductase (SQR) produces sulfane sulfur METPO:2000202

    SQR-catalyzed oxidation of sulfide generates sulfane sulfur intermediates.

    • DOI:10.3390/ijms252010962 Initial oxidation of sulfide occurs under the action of SQR, producing sulfane sulfur; generalizes broadly to intracellular sulfur oxidizers.
  • sulfide:quinone oxidoreductase (SQR) produces polysulfide (H2Sn) METPO:2000202

    SQR oxidizes sulfide to short-chain inorganic polysulfide (H2Sn, n>=2).

    • DOI:10.1128/aem.01941-21 SQR oxidized H2S into short-chain inorganic polysulfide (H2Sn, n >= 2); broad sulfur-chemistry mechanism.
  • polysulfide (H2Sn) precursor of sulfur globule

    Polysulfide/sulfane sulfur spontaneously generates S8 that aggregates into sulfur globules.

    • DOI:10.1128/aem.01941-21 SQR oxidized H2S to H2Sn, which spontaneously generated S8; S8 aggregated into sulfur globules.
  • persulfide dioxygenase (PDO) oxidizes sulfite METPO:2000016

    PDO oxidizes glutathione persulfide (GSSH) to sulfite (GSSH + O2 + H2O -> GSH + SO3^2- + 2H+).

    • DOI:10.3390/ijms252010962 PDO acts on GSSH: GSSH + O2 + H2O -> GSH + SO3^2- + 2H+; well-defined enzymatic edge.

Provenance

Source
METPO (2025-11-25)
Definition source
DOI:10.1016/S0065-2911(08)00002-7

Synonyms (1)

  • sulfur inclusion RELATED_SYNONYM · DOI:10.1016/S0065-2911(08)00002-7

kg-microbe context

Matched 1 kg-microbe node via parent_proxy.

  • METPO:1000059 [-2.682, -2.070, -3.656, -0.652, …]

512-dim DeepWalkSkipGramEnsmallen embedding from kg-microbe (2026-04-25).

Nearest neighbors in embedding space

Top-8 cosine-similar METPO traits from the 2026-04-25 deepwalk (512-D).

Curation history

  1. · PROPOSED_FROM_RESEARCH · claude

    Proposed candidate MORPHOLOGY trait (sulfur globule); storage sub-variant of intracellular inclusion.

  2. · CURATED_CAUSAL_GRAPH · claude

    Added evidence-backed causal graph (oxidative sulfur metabolism → elemental sulfur globule) with METPO/biolink predicate groundings; promoted PROPOSED to REVIEWED.

  3. · GROUND_CAUSAL_NODES · claude

    Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (CHEBI:26833×1).

  4. · ENRICH_CAUSAL_GRAPH · claude

    Added 4 evidence-backed generic edges (5 new nodes) from the deep-research report.

  5. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 3 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (METPO:2000202×2, METPO:2000016×1).