Sulfhydryl groups, disulfide bridges and the state of copper in three blue oxidases
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(75)80851-9/fullpdf
Reference20 articles.
1. Oxidation-reduction potentials of the electron acceptors in laccases and stellacyanin
2. Anion-binding and the state of copper in caeruloplasmin
3. The stoichiometry of the three different types of copper in ascorbate oxidase from green zucchini squash
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1. Characterization of a laccase gene from the white-rot fungus Trametes versicolor and structural features of basidiomycete laccases;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-09
2. Cloning, sequence analysis, and expression of ligninolytic phenoloxidase genes of the white-rot basidiomycete Coriolus hirsutus.;Journal of Biological Chemistry;1990-09
3. Metal-replacement studies of blue copper proteins;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1983-03
4. Caeruloplasmin: Physiological and Pathological Perspectives;CRC Critical Reviews in Clinical Laboratory Sciences;1981-01
5. Structural studies around cysteine and cystine residues in the “blue” oxidase fungal laccase B. Similarity in amino acid sequence with ceruloplasmin;Biochemical and Biophysical Research Communications;1980-03
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