The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase
Open accessAbstract
The activity of the copper- and zinc-containing superoxide dismutase decreased with increasing ionic strength. Modification of lysine residues by acetylation or succinylation inverted the effect of increasing ionic strength, whereas modification of arginine with phenylglyoxal did not. These results were noted in both photochemical and pulse-radiolysis assays. It appears that interaction of O2- with the anionic enzyme is assisted by the positive charge on lysine residues, presumably those close to the active site. By the criterion of responsiveness to ionic strength, the arginine residue close to the active site does not appear to provide electrostatic facilitation to the catalytic process. Elimination of the charge on epsilon-amino groups by raising the pH suppressed activity to the same extent as did elimination of these charges by acetylation. Activity was similarly suppressed to the same extent by covalent modification or by ionization of arginine residues, indicating that the positive charge on arginine is important for the catalytic process even though its effect is not responsive to changes in the ionic strength of the solution.
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“Several studies have been carried out using pulsed radiolysis to generate HO2•/O2•− and to understand the Cu,Zn-SOD-catalysed reaction of superoxide dismutation [74,75,76,77], Figure 32.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [74]
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Cited by
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Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
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Warshel, A., Sharma, P. K., Kato, M., Xiang, Y., Liu, H., & Olsson, M. H. M. (2006) · Chemical Reviews · doi:10.1021/cr0503106 · Cited by 1,487
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Metadata
- Authors
- Cudd, A., & Fridovich, I.
- Affiliations
- Duke Medical Center (US)
- ORCID
- Cudd, A
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1982-10
- Volume
- 257
- Issue
- 19
- Pages
- 11443-11447
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1592323860
- Cited by
- 211
- References
- 28
- Citations by year
- 2024: 1 · 2023: 1 · 2021: 2 · 2020: 4 · 2019: 4 · 2017: 4 · 2016: 2 · 2015: 3 · 2014: 8 · 2013: 1 · 2012: 2
- FWCI
- 9.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- superoxide dismutase, electrostatic interactions, ionic strength, lysine residues, arginine residues, acetylation, succinylation, phenylglyoxal modification, copper-zinc enzyme, superoxide, enzyme mechanism, pH dependence
- MeSH terms
- Amino Acids, Animals, Cattle, Erythrocytes, Hydrogen-Ion Concentration, Kinetics, Osmolar Concentration, Superoxide Dismutase
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