Single mutations at the subunit interface modulate copper reactivity in Photobacterium leiognathi Cu,Zn superoxide dismutase
- 4 May 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 308 (3) , 555-563
- https://doi.org/10.1006/jmbi.2001.4606
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Cu,Zn Superoxide Dismutase from Photobacterium leiognathi Is an Hyperefficient EnzymeBiochemistry, 1998
- Conserved Enzyme-Substrate Electrostatic Attraction in Prokaryotic Cu,Zn Superoxide DismutasesBiochemical and Biophysical Research Communications, 1998
- Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutaseProceedings of the National Academy of Sciences, 1996
- Modulation of the Catalytic Rate of Cu,Zn Superoxide Dismutase in Single and Double Mutants of Conserved Positively and Negatively Charged ResiduesBiochemistry, 1995
- Simulation of superoxide-superoxide dismutase association rate for six natural variants. Comparison with the experimental catalytic rateThe Journal of Physical Chemistry, 1994
- Faster superoxide dismutase mutants designed by enhancing electrostatic guidanceNature, 1992
- Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site: Evidence for co-ordinated mutation of charged amino acid residuesJournal of Molecular Biology, 1992
- The effects of pH and various salts upon the activity of a series of superoxide dismutasesBiochemical Journal, 1988
- Aspects of the Structure, Function, and Applications of Superoxide DismutasCritical Reviews in Biochemistry, 1987
- Electrostatic recognition between superoxide and copper, zinc superoxide dismutaseNature, 1983