دورية أكاديمية
أعرض في EDS

Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.

التفاصيل البيبلوغرافية
العنوان: Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.
المؤلفون: Azadmanesh J; Eppley Institute for Research in Cancer and Allied Diseases, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA., Slobodnik K; Eppley Institute for Research in Cancer and Allied Diseases, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA., Struble LR; Eppley Institute for Research in Cancer and Allied Diseases, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA., Lutz WE; Eppley Institute for Research in Cancer and Allied Diseases, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA., Coates L; Second Target Station, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37831, USA., Weiss KL; Neutron Scattering Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37831, USA., Myles DAA; Neutron Scattering Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37831, USA., Kroll T; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, 94025, USA., Borgstahl GEO; Eppley Institute for Research in Cancer and Allied Diseases, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA. gborgstahl@unmc.edu.
المصدر: Nature communications [Nat Commun] 2024 Jul 16; Vol. 15 (1), pp. 5973. Date of Electronic Publication: 2024 Jul 16.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: Superoxide Dismutase*/metabolism , Superoxide Dismutase*/chemistry, Humans ; Hydrogen Peroxide/metabolism ; Hydrogen Peroxide/chemistry ; Manganese/metabolism ; Manganese/chemistry ; Electron Transport ; Oxidation-Reduction ; X-Ray Absorption Spectroscopy ; Superoxides/metabolism ; Superoxides/chemistry ; Protons ; Electrons ; Models, Molecular ; Oxygen/metabolism ; Oxygen/chemistry
مستخلص: Human manganese superoxide dismutase (MnSOD) is a crucial oxidoreductase that maintains the vitality of mitochondria by converting superoxide (O 2 ●- ) to molecular oxygen (O 2 ) and hydrogen peroxide (H 2 O 2 ) with proton-coupled electron transfers (PCETs). Human MnSOD has evolved to be highly product inhibited to limit the formation of H 2 O 2 , a freely diffusible oxidant and signaling molecule. The product-inhibited complex is thought to be composed of a peroxide (O 2 2- ) or hydroperoxide (HO 2 - ) species bound to Mn ion and formed from an unknown PCET mechanism. PCET mechanisms of proteins are typically not known due to difficulties in detecting the protonation states of specific residues that coincide with the electronic state of the redox center. To shed light on the mechanism, we combine neutron diffraction and X-ray absorption spectroscopy of the product-bound, trivalent, and divalent states of the enzyme to reveal the positions of all the atoms, including hydrogen, and the electronic configuration of the metal ion. The data identifies the product-inhibited complex, and a PCET mechanism of inhibition is constructed.
(© 2024. The Author(s).)
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معلومات مُعتمدة: P30 CA036727 United States CA NCI NIH HHS; P30 GM133894 United States GM NIGMS NIH HHS; R01 GM145647 United States GM NIGMS NIH HHS
المشرفين على المادة: EC 1.15.1.1 (Superoxide Dismutase)
BBX060AN9V (Hydrogen Peroxide)
42Z2K6ZL8P (Manganese)
11062-77-4 (Superoxides)
0 (Protons)
S88TT14065 (Oxygen)
تواريخ الأحداث: Date Created: 20240716 Date Completed: 20240716 Latest Revision: 20240725
رمز التحديث: 20240726
مُعرف محوري في PubMed: PMC11252399
DOI: 10.1038/s41467-024-50260-w
PMID: 39013847
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-024-50260-w