Kinetic and magnetic resonance studies of substrate binding to galactose oxidase copper(II)
- 1 January 1981
- journal article
- research article
- Published by Elsevier in Journal of Inorganic Biochemistry
- Vol. 14 (3) , 223-235
- https://doi.org/10.1016/s0162-0134(00)80002-1
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Magnetic resonance studies of cyanide and fluoride binding to galactose oxidase copper(II): evidence for two exogenous ligand sitesJournal of the American Chemical Society, 1981
- Kinetic mechanism of the Cu(II) enzyme galactose oxidaseJournal of Inorganic Biochemistry, 1981
- o,o-Dityrosine in native and horseradish peroxidase-activated galactose oxidaseBiochemical and Biophysical Research Communications, 1980
- Fluoride ion as a nuclear magnetic resonance probe of galactose oxidase. An analysis of the fluorine-19 nuclear magnetic resonance relaxation ratesThe Journal of Physical Chemistry, 1979
- An example of pseudo five-coordination in copper(II) complexesInorganic Chemistry, 1979
- Role of tryptophan in the spectral and catalytic properties of the copper enzyme, galactose oxidaseBiochemistry, 1977
- Fluorescence properties of the copper enzyme galactose oxidase and its tryptophan-modified derivativesBiochemistry, 1977
- Circular dichroism spectra of the copper enzyme, galactose oxidase, in the presence of its substrates and productsBiochemistry, 1974
- Stereoelectronic properties of metalloenzymes. II. Effects of ligand coordination on the electron spin resonance spectrum of galactose oxidase as a probe of structure and functionJournal of the American Chemical Society, 1974
- Nuclear Magnetic Relaxation of 19F Due to Cu(II) in Aqueous Solutions of F− and HFThe Journal of Chemical Physics, 1968