DOE PAGES title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: 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:
 [1]
  1. 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}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 1 work
Citation information provided by
Web of Science

Save / Share:

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
  • DOI: 10.1016/j.bbadis.2011.12.002

Superoxide Dismutases and Superoxide Reductases
journal, January 2014

  • Sheng, Yuewei; Abreu, Isabel A.; Cabelli, Diane E.
  • Chemical Reviews, Vol. 114, Issue 7
  • DOI: 10.1021/cr4005296

Superoxide dismutase activity enabled by a redox-active ligand rather than metal
journal, October 2018


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
  • DOI: 10.1016/j.bbamcr.2006.05.003