Conserved Enzyme-Substrate Electrostatic Attraction in Prokaryotic Cu,Zn Superoxide Dismutases
โ Scribed by Silvia Folcarelli; Andrea Battistoni; Mattia Falconi; Peter O'Neill; Giuseppe Rotilio; Alessandro Desideri
- Book ID
- 115581843
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 131 KB
- Volume
- 244
- Category
- Article
- ISSN
- 0006-291X
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## Abstract We have expressed and characterized a mutant of __Xenopus laevis__ Cu, Zn superoxide dismutase in which four highly conserved charged residues belonging to the electrostatic loop have been replaced by neutral side chains: Lys120 โ Leu, Asp130 โ Gln, Glu131 โ Gln, and Lys134 โ Thr. At lo
We used Brownian dynamics simulations of substrate 0, encounters with the enzyme bovine erythrocyte Cu, Zn superoxide dismutase (SOD) to study the effects of multiple charge modifications in the enzyme on the kinetics of its diffusion-controlled reaction. When the charges of two or three residues we