دورية أكاديمية
أعرض في EDS

The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.

التفاصيل البيبلوغرافية
العنوان: The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.
المؤلفون: Yoo BK; Laboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu., Kruglik SG; Laboratoire Jean Perrin, Institut de Biologie Paris-Seine, Sorbonne Université, CNRS 75005 Paris France., Lambry JC; Laboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu., Lamarre I; Laboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu., Raman CS; Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland Baltimore Maryland 21201 USA., Nioche P; Environmental Toxicity, Therapeutic Targets, Cellular Signaling and Biomarkers, UMR S1124, Centre Universitaire des Saints-Pères, Université Paris Descartes 75006 Paris France.; Structural and Molecular Analysis Platform, BioMedTech Facilities, INSERM US36-CNRS-UMS2009, Paris Université Paris France., Negrerie M; Laboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu.
المصدر: Chemical science [Chem Sci] 2023 Jul 13; Vol. 14 (31), pp. 8408-8420. Date of Electronic Publication: 2023 Jul 13 (Print Publication: 2023).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 101545951 Publication Model: eCollection Cited Medium: Print ISSN: 2041-6520 (Print) Linking ISSN: 20416520 NLM ISO Abbreviation: Chem Sci Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : Royal Society of Chemistry, [2010]-
مستخلص: Some classes of bacteria within phyla possess protein sensors identified as homologous to the heme domain of soluble guanylate cyclase, the mammalian NO-receptor. Named H-NOX domain (Heme-Nitric Oxide or OXygen-binding), their heme binds nitric oxide (NO) and O 2 for some of them. The signaling pathways where these proteins act as NO or O 2 sensors appear various and are fully established for only some species. Here, we investigated the reactivity of H-NOX from bacterial species toward NO with a mechanistic point of view using time-resolved spectroscopy. The present data show that H-NOXs modulate the dynamics of NO as a function of temperature, but in different ranges, changing its affinity by changing the probability of NO rebinding after dissociation in the picosecond time scale. This fundamental mechanism provides a means to adapt the heme structural response to the environment. In one particular H-NOX sensor the heme distortion induced by NO binding is relaxed in an ultrafast manner (∼15 ps) after NO dissociation, contrarily to other H-NOX proteins, providing another sensing mechanism through the H-NOX domain. Overall, our study links molecular dynamics with functional mechanism and adaptation.
Competing Interests: There are no conflicts to declare.
(This journal is © The Royal Society of Chemistry.)
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تواريخ الأحداث: Date Created: 20230811 Latest Revision: 20230812
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC10411614
DOI: 10.1039/d3sc01685d
PMID: 37564404
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-6520
DOI:10.1039/d3sc01685d