{
  "abstract": "Macromolecular crowding has long been known to alter biochemical equilibria and enzyme kinetics, with reported catalytic activities that may increase, decrease, or vary non-monotonically with crowder concentration. Classical Michaelis--Menten kinetics does not by itself identify which of these responses should occur for a conformationally active enzyme. Here, we develop a minimal non-equilibrium mechano-chemical theory for a fueled enzyme embedded in a bath of passive crowders and uncover a fluctuation-induced effective force dipole acting on the enzyme subunits, akin to a generalized form of dispersion or depletion interaction. Since the preferred conformation of the model enzyme varies through the catalytic cycle, the fluctuation-induced mechanical load affects the relevant kinetic activation barriers and is sufficient to produce both monotonic inhibition and non-monotonic modification of turnover. The framework provides a thermodynamically consistent route for linking crowded environments to catalytic currents, suggesting how mechanical design principles could be leveraged to control enzymatic pathways.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": "2611.03239",
  "author_total": 4,
  "authors": [
    {
      "name": "Michalis Chatzittofi"
    },
    {
      "name": "Luca Cocconi"
    },
    {
      "name": "Jakob Metson"
    },
    {
      "name": "Ramin Golestanian"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/34bvqa85r2em5.bib",
  "cited_by": 0,
  "doi": "10.48550/arxiv.2611.03239",
  "fulltext_url": null,
  "id": "34bvqa85r2em5",
  "issns": [],
  "landing_url": "https://arxiv.org/abs/2611.03239",
  "language": null,
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "http://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": "CC0-1.0",
  "native_subjects": [
    [
      "arxiv",
      "cond-mat.soft"
    ],
    [
      "arxiv",
      "cond-mat.stat-mech"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://arxiv.org/pdf/2611.03239",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-02",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/34bvqa85r2em5.ris",
  "sources": [
    {
      "first_seen": "2026-11-03T12:21:04Z",
      "native_id": "2611.03239",
      "source": "arxiv",
      "url": "https://arxiv.org/abs/2611.03239"
    }
  ],
  "subjects": [
    {
      "field": "physics",
      "origin": "arxiv:cond-mat.soft",
      "subfield": "condensed-matter"
    },
    {
      "field": "physics",
      "origin": "arxiv:cond-mat.stat-mech",
      "subfield": "statistical-nonlinear"
    }
  ],
  "title": "Mechano-chemical control of enzymatic activity in crowded environments",
  "title_text": "Mechano-chemical control of enzymatic activity in crowded environments",
  "type": "preprint",
  "updated_at": "2026-11-05T15:20:21Z",
  "url": "https://research.draconitic.com/paper/34bvqa85r2em5",
  "venue": "arXiv",
  "versions": []
}