EPR Studies on a Stable Sulfinyl Radical Observed in the Iron−Oxygen-Reconstituted Y177F/I263C Protein R2 Double Mutant of Ribonucleotide Reductase from Mouse-Reference-Cited by-同舟云学术

EPR Studies on a Stable Sulfinyl Radical Observed in the Iron−Oxygen-Reconstituted Y177F/I263C Protein R2 Double Mutant of Ribonucleotide Reductase from Mouse

Published:2002-04-26 Issue:20 Volume:41 Page:6510-6516
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Adrait Annie¹,Öhrström Maria¹,Barra Anne-Laure¹,Thelander Lars¹,Gräslund Astrid¹

Affiliation:

1. Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-106 91 Stockholm, Sweden, The High Magnetic Field Laboratory, CNRS/MPI, F-38042 Grenoble Cedex, France, and Department of Medical Biochemistry and Biophysics, Umeå University, SE−901 87 Umeå, Sweden

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi012043d

Reference53 articles.

1. Sjöberg, B.M. (1995) inNucleic Acids and Molecular Biology(Eckstein, F., and Lilley, D. M. J., Eds.) Vol. 9, pp 192−221, Springer-Verlag, Berlin.

2. Sahlin, M., and Sjöberg, B.M. (2000) inSubcellular Biochemistry(Holzenburg and Scrutton, Eds.) Vol. 35, pp 405−443, Kluwer Academic/Plenum Publishers, New York.

3. Identification of the stable free radical tyrosine residue in ribonucleotide reductase.

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