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An electrostatic enzyme-substrate recognition: the case of Cu, Zn superoxide dismutase

✍ Scribed by Alessandro Desideri; Fabio Polticelli; Mattia Falconi

Book ID
113257763
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
591 KB
Volume
256
Category
Article
ISSN
0166-1280

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πŸ“œ SIMILAR VOLUMES

Role of the electrostatic loop charged r
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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Cu, Zn superoxide dismutase in which four highly conserved charged residues belonging to the electrostatic loop have been replaced by neutral side chains: Lys120 β†’ Leu, Asp130 β†’ Gln, Glu131 β†’ Gln, and Lys134 β†’ Thr. At lo

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Atomic partial charges for three model systems that mimic the metal-ligand moiety of the active site in the enzyme Cu, Zn superoxide dismutase (SOD) have been calculated at the ab initio level. The model systems include copper and zinc complexes with imidazole, formate and ammonia ligands. The parti

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