Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit (Q70267348)

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scientific article published on July 15, 1983

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English	Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit	scientific article published on July 15, 1983

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scholarly article

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10 October 2019

Hydroperoxide anion, HO-2, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: modification of one histidine per subunit (English)

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10 October 2019

Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit (English)

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10.1016/0003-9861(83)90245-X

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4 October 2023

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4 October 2023

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D. M. Blech

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4 October 2023

C. L. Borders

2

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1 July 1983

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10 October 2019

15 July 1983

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National Center for Biotechnology Information

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=6347073

4 October 2023

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https://api.elsevier.com/content/article/PII:000398618390245X?httpAccept=text/plain

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Archives of Biochemistry and Biophysics

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10 October 2019

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10 October 2019

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10 October 2019

579-586

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10 October 2019

Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase

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Reduction and inactivation of superoxide dismutase by hydrogen peroxide

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Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase

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Reversal of the superoxide dismutase reaction

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Identification of Arg-143 as the essential arginyl residue in yeast Cu,Zn superoxide dismutase by use of a chromophoric arginine reagent

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Kinetic study of O-2 DISMUTATION BY BOVINE SUPEROXIDE DISMUTASE. Evidence for saturation of the catalytic sites by O-2.

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A water 17O NMR study of the pH dependent properties of superoxide dismutase

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Arginyl Residues: Anion Recognition Sites in Enzymes

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Identifiers

10.1016/0003-9861(83)90245-X

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6347073%20AND%20SRC:MED&resulttype=core&format=json

10 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6347073%20AND%20SRC:MED&resulttype=core&format=json

10 October 2019

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