Ab Initio Study of the Mechanism of the Binding of Triplet O2 to Hemocyanin
- 1 January 1996
- journal article
- Published by American Chemical Society (ACS) in Inorganic Chemistry
- Vol. 35 (18) , 5207-5212
- https://doi.org/10.1021/ic960102j
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Active sites in copper proteins an electronic structure overviewPublished by Springer Nature ,2007
- Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differencesProteins-Structure Function and Bioinformatics, 1994
- An electronic structural comparison of copper-peroxide complexes of relevance to hemocyanin and tyrosinase active sitesJournal of the American Chemical Society, 1991
- Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolutionJournal of Molecular Biology, 1989
- Extended X-ray absorption fine structure study of the coupled binuclear copper active site of tyrosinase from Neurospora crassaBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Electronic and geometric structure-function correlations of the coupled binuclear copper active sitePublished by Walter de Gruyter GmbH ,1983
- Chemical and spectroscopic studies of the binuclear copper active site of Neurospora tyrosinase: comparison to hemocyaninsJournal of the American Chemical Society, 1980
- Structural studies of the hemocyanin active site. 2. Resonance Raman spectroscopyJournal of the American Chemical Society, 1980
- A resonance Raman study of the copper protein, hemocyanin. New evidence for the structure of the oxygen-binding siteJournal of the American Chemical Society, 1976
- Oxygen binding to hemocyanin: A resonance raman spectroscopic studyBiochemical and Biophysical Research Communications, 1974