Mutation of Lys-120 and Lys-134 drastically reduces the catalytic rate of Cu,Zn superoxide dismutase

Fabio Polticelli, Andrea Battistoni, Grazia Bottaro, Maria Teresa Carri, Peter O'Neill, Alessandro Desideri, Giuseppe Rotilio

Research output: Contribution to journalArticlepeer-review

Abstract

Lys-120 and Lys-134, located at the edge of the active site channel in most Cu,Zn superoxide dismutases, have been suggested to play a major role in steering the anionic substrate towards the catalytic copper ion. In this study, mutants of Xenopus laevis Cu,Zn superoxide dismutase have been engineered, with Lys-120 and Lys-134 changed into leucine and threonine, respectively, and their catalytic properties have been investigated by pulse radiolysis. Results obtained demonstrate that both residues decrease the catalytic rate by about 40%, in partial disagreement with previous brownian dynamics calculations, carried out on bovine Cu,Zn superoxide dismutase.

Original languageEnglish
Pages (from-to)76-78
Number of pages3
JournalFEBS Letters
Volume352
Issue number1
DOIs
Publication statusPublished - Sep 19 1994

Keywords

  • Brownian dynamics
  • Electrostatic interaction
  • Pulse radiolysis
  • Site-directed mutagenesis
  • Superoxide dismutase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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