Engineering type 1 copper sites in proteins
- 28 June 1993
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 325 (1-2), 39-48
- https://doi.org/10.1016/0014-5793(93)81410-2
Abstract
The use of site-directed mutagenesis methods has revolutionalized the study of the so-called type 1 and type 2 copper sites in proteins. In particular our understanding of the relation between the structure, and the mechanistic and spectroscopic features of these sites is benefitting from the application of these techniques. Recent progress in the field is reviewed with emphasis on the study of type 1 sites. Topics covered comprise the characteristics of the natural type 1 and type 2 sites, the genetics of blue copper proteins, the modification of Cu sites, the spectroscopy of natural and engineered type 1 and type 2 sites, the effect of mutations on midpoint potentials and the mechanism of electron transfer as carried out by the blue copper proteins.Keywords
This publication has 71 references indexed in Scilit:
- Three-dimensional model for stellacyanin, a “blue” copper-proteinJournal of Molecular Biology, 1991
- Construction of new ligand binding sites in proteins of known structureJournal of Molecular Biology, 1991
- Flash‐photolysis studies of the electron transfer from genetically modified spinach plastocyanin to photosystem IFEBS Letters, 1991
- Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacteriumextorquens AM1: Evidence for two tryptophan residues involved in the active centerBiochemical and Biophysical Research Communications, 1990
- Effect of NO2-modification of Tyr83 on the reactivity of spinach plastocyanin with inorganic redox partners [Fe(CN)6]3−/4− and [Co(phen)3]3+/2+Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- The azurin gene from Pseudomonas aeruginosa codes for a pre‐protein with a signal peptideFEBS Letters, 1987
- Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH valuesJournal of Molecular Biology, 1986
- The pH and redox-state dependence of the copper site in azurin from Pseudomonas aeruginosa as studied by EXAFSBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Structure of azurin from Alcaligenes denitrificans at 2·5 Å resolutionJournal of Molecular Biology, 1983
- Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutaseJournal of Molecular Biology, 1982