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Title: Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction

Abstract

Human manganese superoxide dismutase (MnSOD) is one of the most significant enzymes in preventing mitochondrial dysfunction and related diseases by combating reactive oxygen species (ROS) in the mitochondrial matrix. Mitochondria are the source of up to 90% of cellular ROS generation, and MnSOD performs its necessary bioprotective role by converting superoxide into oxygen and hydrogen peroxide. This vital catalytic function is conducted via cyclic redox reactions between the substrate and the active-site manganese using proton-coupled electron transfers. Owing to protons being difficult to detect experimentally, the series of proton transfers that compose the catalytic mechanism of MnSOD are unknown. Here, methods are described to discern the proton-based mechanism using chemical treatments to control the redox state of large perdeuterated MnSOD crystals and subsequent neutron diffraction. These methods could be applicable to other crystal systems in which proton information on the molecule in question in specific chemical states is desired.

Authors:
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Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1471802
Resource Type:
Published Article
Journal Name:
Acta Crystallographica Section F Structural Biology Communications
Additional Journal Information:
Journal Name: Acta Crystallographica Section F Structural Biology Communications Journal Volume: 74 Journal Issue: 10; Journal ID: ISSN 2053-230X
Publisher:
International Union of Crystallography (IUCr)
Country of Publication:
United Kingdom
Language:
English

Citation Formats

Azadmanesh, Jahaun, Lutz, William E., Weiss, Kevin L., Coates, Leighton, and Borgstahl, Gloria E. O. Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction. United Kingdom: N. p., 2018. Web. doi:10.1107/S2053230X18011299.
Azadmanesh, Jahaun, Lutz, William E., Weiss, Kevin L., Coates, Leighton, & Borgstahl, Gloria E. O. Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction. United Kingdom. doi:10.1107/S2053230X18011299.
Azadmanesh, Jahaun, Lutz, William E., Weiss, Kevin L., Coates, Leighton, and Borgstahl, Gloria E. O. Fri . "Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction". United Kingdom. doi:10.1107/S2053230X18011299.
@article{osti_1471802,
title = {Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction},
author = {Azadmanesh, Jahaun and Lutz, William E. and Weiss, Kevin L. and Coates, Leighton and Borgstahl, Gloria E. O.},
abstractNote = {Human manganese superoxide dismutase (MnSOD) is one of the most significant enzymes in preventing mitochondrial dysfunction and related diseases by combating reactive oxygen species (ROS) in the mitochondrial matrix. Mitochondria are the source of up to 90% of cellular ROS generation, and MnSOD performs its necessary bioprotective role by converting superoxide into oxygen and hydrogen peroxide. This vital catalytic function is conducted via cyclic redox reactions between the substrate and the active-site manganese using proton-coupled electron transfers. Owing to protons being difficult to detect experimentally, the series of proton transfers that compose the catalytic mechanism of MnSOD are unknown. Here, methods are described to discern the proton-based mechanism using chemical treatments to control the redox state of large perdeuterated MnSOD crystals and subsequent neutron diffraction. These methods could be applicable to other crystal systems in which proton information on the molecule in question in specific chemical states is desired.},
doi = {10.1107/S2053230X18011299},
journal = {Acta Crystallographica Section F Structural Biology Communications},
number = 10,
volume = 74,
place = {United Kingdom},
year = {2018},
month = {9}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.1107/S2053230X18011299

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