{
  "abstract": "Heme serves as a crucial cofactor for hemoproteins and as an iron reservoir; yet, its accumulation is toxic, necessitating efficient degradation pathways. While the catabolism of free heme b is well characterized, the enzymes that disrupt its counterpart covalently tethered to a peptide (heme c) have remained elusive. Here, through a pipeline of multiple in silico analyses, we predict a distinct Core-only type of heme oxygenases (HOs) within the HugZ superfamily to have the potential to degrade both heme b and peptide-tethered heme c. Biochemical and physiological characterization confirms that representative Core-only-type HOs confer balanced dual-substrate specificity. In contrast, the C-extension and N-fusion-type HOs degrade heme b, but not heme c, because the entry of heme c into the active pocket is blocked by their extra domains. Moreover, we show that the degradation of heme c by the Core-only-type HOs requires proteolytic digestion of heme c-carrying proteins by a protease such as DegQ, which occurs in the periplasm. Overall, this work provides an integrated evolutionary, structural, biochemical, and physiological framework that defines a novel strategy for heme recycling and adaptive metabolic flexibility in bacteria.",
  "abstract_shown": true,
  "affiliations": [
    "Institute of Microbiology, College of Life Sciences Zhejiang University Hangzhou China.",
    "State Key Laboratory for Vegetation Structure Function and Construction (VegLab), College of Life Sciences Zhejiang University Hangzhou China."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "affs": [
        0,
        1
      ],
      "name": "Jiyuan Hou"
    },
    {
      "affs": [
        0
      ],
      "name": "Wenhan Dong"
    },
    {
      "affs": [
        0
      ],
      "name": "Hui Yang"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Yuxuan Liang"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Haichun Gao",
      "orcid": "0000-0002-2647-6563"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/3amem2nj8kqhg.bib",
  "cited_by": 0,
  "doi": "10.1002/mlf2.70118",
  "fulltext_url": "https://europepmc.org/articles/PMC13715372",
  "id": "3amem2nj8kqhg",
  "issns": [
    "2097-1699",
    "2770-100X"
  ],
  "landing_url": "https://europepmc.org/article/MED/42953331",
  "language": "eng",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "heading",
      "Original Research"
    ],
    [
      "openalex",
      "1312|Heme Oxygenase-1 and Carbon Monoxide"
    ]
  ],
  "openalex": "W7224129111",
  "pdf_url": "https://europepmc.org/articles/PMC13715372?pdf=render",
  "pmcid": "PMC13715372",
  "pmid": "42953331",
  "published": "2026-10-28",
  "publisher": "Wiley",
  "ris": "https://research.draconitic.com/paper/3amem2nj8kqhg.ris",
  "sources": [
    {
      "first_seen": "2026-10-31T00:20:40Z",
      "native_id": "MED:42953331",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42953331"
    },
    {
      "first_seen": "2026-11-02T12:23:15Z",
      "native_id": "PMC13715372",
      "source": "pmc",
      "url": "https://doi.org/10.1002/mlf2.70118"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Heme Oxygenase-1 and Carbon Monoxide",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Capture of long-missing heme oxygenases that degrade both heme b and heme c.",
  "title_text": "Capture of long-missing heme oxygenases that degrade both heme b and heme c.",
  "type": "peer-reviewed",
  "updated_at": "2026-11-03T12:20:21Z",
  "url": "https://research.draconitic.com/paper/3amem2nj8kqhg",
  "venue": "MLife",
  "versions": []
}