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

Access to Document

10.1016/0014-5793(94)00885-X

Cite this

@article{1e425b191ea34c1389665f7fc193ed81,

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",

month = sep,

day = "19",

doi = "10.1016/0014-5793(94)00885-X",

language = "English",

volume = "352",

pages = "76--78",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

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

UR - http://www.scopus.com/inward/record.url?scp=0028167858&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028167858&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(94)00885-X

DO - 10.1016/0014-5793(94)00885-X

M3 - Article

C2 - 7925948

AN - SCOPUS:0028167858

VL - 352

SP - 76

EP - 78

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this