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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Cites
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Self-citationSuperoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Self-citationCatalysis in chemistry and enzymology
Jencks, W. P. (1969) · Medical Entomology and Zoology · Cited by 3,217
Chemical Modification of Proteins
Roberts, G. C. K. (2012) · Springer eBooks · doi:10.1007/978-3-642-16712-6_100145 · Cited by 1,074
Hirs, C. H. W. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(67)11021-5 · Cited by 867
The Reaction of Phenylglyoxal with Arginine Residues in Proteins
Takahashi, K. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94475-3 · Cited by 650
Study of the Dansylation Reaction of Amino Acids, Peptides and Proteins
Gros, C. P., & Labouesse, B. (1969) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1969.tb19632.x · Cited by 594
Oxygen and oxy‐radicals in chemistry and biology
Halliwell, B. B. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80255-x · Cited by 553
Klug-Roth, D., Rabani, J., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44987-9 · Cited by 495
Self-citationChemical Modification of Proteins
Wood, E. (1974) · Biochemical Education · doi:10.1016/0307-4412(74)90019-3 · Cited by 404
Research works printed but not linked: 3
- Fridovich, 1974, Adv. Enzymol. Relat. Areas Mol. Biol., 41, 33
- Tainer, 1982, J. Mol. Biol.
- Cass, 1978, Carlsberg Res. Commun., 64, 429
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Items 201–211 of 211
Cabelli, D. E. (2010) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814282093_0017
スーパーオキサイド (O2-) とNOとの関係からみた細胞障害
博江, 中., 直人, 福., 源河, 朝., 星合, 清., Zhi, S., & 英之, 石. (1998) · 蘇生 · doi:10.11414/jjreanimatology1983.17.1
Vassall, K. A. (2009) · UWSpace (University of Waterloo)
Grotemeyer, E. N., & Jackson, T. A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14851-6
Kojda, G. (2001) · Steinkopff eBooks · doi:10.1007/978-3-642-87803-9_1
Brooks, C. L., Karplus, M., & Pettitt, B. M. (1988) · Advances in chemical physics · doi:10.1002/9780470141205.refs
Oxidative Stress in Familial Amyotrophic Lateral Sclerosis
Cabelli, D. E. (2003) · Oxidative stress and disease · doi:10.1201/9780203912874.ch21
Mechanismen potenziell vasoprotektiver Wirkungen von NO
Kojda, G. (2001) · Steinkopff eBooks · doi:10.1007/978-3-642-87803-9_3
Effects of aging and physical activity on superoxide dismutase in human erythrocytes
Manhas, S. K. (1994) · Summit (Simon Fraser University)
Der NO/cGMP-Signaltransduktionsweg
Kojda, G. (2001) · Steinkopff eBooks · doi:10.1007/978-3-642-87803-9_2
Vakser (1996) · doi:10.1002/(sici)1097-0282(199609)39:3
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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