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

doi:10.1016/0014-5793(94)00885-X

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

Fondazione Santa Lucia

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	76-78
Number of pages	3
Journal	FEBS Letters
Volume	352
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(94)00885-X
Publication status	Published - 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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title = "Mutation of Lys-120 and Lys-134 drastically reduces the catalytic rate of Cu,Zn superoxide dismutase",

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.",

keywords = "Brownian dynamics, Electrostatic interaction, Pulse radiolysis, Site-directed mutagenesis, Superoxide dismutase",

author = "Fabio Polticelli and Andrea Battistoni and Grazia Bottaro and Carri, {Maria Teresa} and Peter O'Neill and Alessandro Desideri and Giuseppe Rotilio",

year = "1994",

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T1 - Mutation of Lys-120 and Lys-134 drastically reduces the catalytic rate of Cu,Zn superoxide dismutase

AU - Polticelli, Fabio

AU - Battistoni, Andrea

AU - Bottaro, Grazia

AU - Carri, Maria Teresa

AU - O'Neill, Peter

AU - Desideri, Alessandro

AU - Rotilio, Giuseppe

PY - 1994/9/19

Y1 - 1994/9/19

N2 - 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.

AB - 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.

KW - Brownian dynamics

KW - Electrostatic interaction

KW - Pulse radiolysis

KW - Site-directed mutagenesis

KW - Superoxide dismutase

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