Redox activity goes organic [Superoxide dismutase mimics: Redox activity goes organic]
Abstract
Superoxide dismutase mimics can help regulate the levels of O2•– in the body, but typically rely on redox-active metals that are toxic in their free form. Here, a complex featuring a redox-active quinol moiety complexed to a redox-inactive zinc centre has been shown to catalyse O2•– dismutation.
- Authors:
-
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Publication Date:
- Research Org.:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1491151
- Report Number(s):
- BNL-210858-2019-JAAM
Journal ID: ISSN 1755-4330
- Grant/Contract Number:
- SC0012704
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Chemistry
- Additional Journal Information:
- Journal Volume: 10; Journal Issue: 12; Journal ID: ISSN 1755-4330
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 38 RADIATION CHEMISTRY, RADIOCHEMISTRY, AND NUCLEAR CHEMISTRY
Citation Formats
Cabelli, Diane E. Redox activity goes organic [Superoxide dismutase mimics: Redox activity goes organic]. United States: N. p., 2018.
Web. doi:10.1038/s41557-018-0180-y.
Cabelli, Diane E. Redox activity goes organic [Superoxide dismutase mimics: Redox activity goes organic]. United States. https://doi.org/10.1038/s41557-018-0180-y
Cabelli, Diane E. Wed .
"Redox activity goes organic [Superoxide dismutase mimics: Redox activity goes organic]". United States. https://doi.org/10.1038/s41557-018-0180-y. https://www.osti.gov/servlets/purl/1491151.
@article{osti_1491151,
title = {Redox activity goes organic [Superoxide dismutase mimics: Redox activity goes organic]},
author = {Cabelli, Diane E.},
abstractNote = {Superoxide dismutase mimics can help regulate the levels of O2•– in the body, but typically rely on redox-active metals that are toxic in their free form. Here, a complex featuring a redox-active quinol moiety complexed to a redox-inactive zinc centre has been shown to catalyse O2•– dismutation.},
doi = {10.1038/s41557-018-0180-y},
journal = {Nature Chemistry},
number = 12,
volume = 10,
place = {United States},
year = {Wed Nov 21 00:00:00 EST 2018},
month = {Wed Nov 21 00:00:00 EST 2018}
}
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Works referenced in this record:
Manganese superoxide dismutase, MnSOD and its mimics
journal, May 2012
- Miriyala, Sumitra; Spasojevic, Ivan; Tovmasyan, Artak
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, Vol. 1822, Issue 5
Superoxide Dismutases and Superoxide Reductases
journal, January 2014
- Sheng, Yuewei; Abreu, Isabel A.; Cabelli, Diane E.
- Chemical Reviews, Vol. 114, Issue 7
Superoxide dismutase activity enabled by a redox-active ligand rather than metal
journal, October 2018
- Ward, Meghan B.; Scheitler, Andreas; Yu, Meng
- Nature Chemistry, Vol. 10, Issue 12
Activation of superoxide dismutases: Putting the metal to the pedal
journal, July 2006
- Culotta, Valeria Cizewski; Yang, Mei; O'Halloran, Thomas V.
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol. 1763, Issue 7