Structure of the active site of hemocyanin. Cobalt(II)-substituted squid hemocyanin
Author:
Publisher
Elsevier BV
Subject
Materials Chemistry,Inorganic Chemistry,Physical and Theoretical Chemistry
Reference44 articles.
1. Structure and Function of Haemocyanin;Lontie,1977
2. A resonance Raman study of the copper protein, hemocyanin. New evidence for the structure of the oxygen-binding site
3. Resonance Raman study of oxyhemocyanin with unsymmetrically labeled oxygen
4. Structural studies of the hemocyanin active site. 1. Extended x-ray absorption fine structure (EXAFS) analysis
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1. Spectroscopic distinction between two Co(II) ions substituted for types 1 and 2 Cu in nitrite reductase;Inorganica Chimica Acta;1998-07
2. Cobalt(II) Substituted Derivatives of Carcinus maenas Hemocyanin: Magnetic Characterization, Magnetooptic, and Kinetic Studies Regarding the Geometry of the Active Site;Inorganic Chemistry;1996-01-01
3. Activation of Dioxygen by Cobalt Group Metal Complexes;Advances in Inorganic Chemistry;1996
4. An x-ray absorption near edge structure spectroscopy study of metal coordination in Co(II)-substituted Carcinus maenas hemocyanin;Biophysical Journal;1993-12
5. The Binding of Cd(II) to the Hemocyanin of the Mediterranean Crab Carcinus maenas;Archives of Biochemistry and Biophysics;1993-04
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