Efficiency of nitrilotriacetate in the removal of type 2 copper from laccase and ascorbate oxidase
- 16 July 1990
- journal article
- Published by Elsevier in Inorganica Chimica Acta
- Vol. 173 (2) , 261-264
- https://doi.org/10.1016/s0020-1693(00)80222-4
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- copper proteins systems containing the “Blue” copper centerPublished by Springer Nature ,2007
- X-ray crystal structure of the blue oxidase ascorbate oxidase from ZucchiniJournal of Molecular Biology, 1989
- Reassessment of copper stoichiometry in ascorbate oxidaseBiochemical and Biophysical Research Communications, 1988
- Low-temperature magnetic circular dichroism studies of native laccase: confirmation of a trinuclear copper active siteJournal of the American Chemical Society, 1986
- Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site.Proceedings of the National Academy of Sciences, 1985
- Heterogeneity of the Type 3 copper in Japanese-lacquer-tree (Rhus vernicifera) laccaseBiochemical Journal, 1982
- Type 2 copper(II) as a component of the dioxygen reducing site in laccase: Evidence from EPR experiments with 17OFEBS Letters, 1977
- Selective removal of type 2 copper from Rhus vernicifera laccaseFEBS Letters, 1976
- Purification and properties of laccase and stellacyanin from Rhus verniciferaBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1970
- Mobilization of iron from ferritin by chelating agentsBiochemistry, 1968