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
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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 -