Literature DB >> 1649093

Advances in the understanding of the structure-function relationship in Cu,Zn superoxide dismutase.

L Banci1, I Bertini, D E Cabelli, R A Hallewell, C Luchinat, M S Viezzoli.   

Abstract

The structure-function relationship in Cu,Zn superoxide dismutase has been partially elucidated by the combined use of many spectroscopic techniques (electronic spectroscopy, circular dichroism, EPR and NMR) and site-directed mutagenesis techniques. The comparison of the spectroscopic and catalytic properties of various mutants, in which some active site residues have been substituted through site-directed mutagenesis, allowed us to establish that the activity is in general more sensitive to electrostatic effects rather than to steric effects or changes in the copper hydration or coordination geometry.

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Year:  1991        PMID: 1649093     DOI: 10.3109/10715769109145792

Source DB:  PubMed          Journal:  Free Radic Res Commun        ISSN: 8755-0199


  4 in total

Review 1.  The structural biochemistry of the superoxide dismutases.

Authors:  J J P Perry; D S Shin; E D Getzoff; J A Tainer
Journal:  Biochim Biophys Acta       Date:  2009-11-13

2.  Role of conserved tyrosine residues in NiSOD catalysis: a case of convergent evolution.

Authors:  Robert W Herbst; Abigail Guce; Peter A Bryngelson; Khadine A Higgins; Kelly C Ryan; Diane E Cabelli; Scott C Garman; Michael J Maroney
Journal:  Biochemistry       Date:  2009-04-21       Impact factor: 3.162

3.  Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii that is active with iron or manganese: pH-dependence.

Authors:  B Meier; C Michel; M Saran; J Hüttermann; F Parak; G Rotilio
Journal:  Biochem J       Date:  1995-09-15       Impact factor: 3.857

4.  A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase.

Authors:  I Bertini; M Piccioli; M S Viezzoli; C Y Chiu; G T Mullenbach
Journal:  Eur Biophys J       Date:  1994       Impact factor: 1.733

  4 in total

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