The reaction of Octopus vulgaris hemocyanin with exogenous ligands: Proposal of an allosteric model for the binding of cyanide and thiourea to the 11 S subunit-Reference-Cited by-同舟云学术

The reaction of Octopus vulgaris hemocyanin with exogenous ligands: Proposal of an allosteric model for the binding of cyanide and thiourea to the 11 S subunit

Published:1988-11 Issue:2 Volume:266 Page:539-547
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Giacometti Giorgio M.,di Muro Paolo,Salvato Benedetto,Beltramini Mariano

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference32 articles.

1. copper proteins systems containing the “Blue” copper center

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

5. Copper Proteins;Solomon,1981

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1. Type-3 copper proteins as biocompatible and reusable oxygen sensors;Inorganica Chimica Acta;2008-03

2. Dissociation kinetics of hemocyanin from Octopus vulgaris;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1998-06

3. Biochemical and functional characterization of Rapana thomasiana hemocyanin;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1991-01

4. The reaction of CN− with the binuclear copper site of Neurospora tyrosinase: its relevance for a comparison between tyrosinase and hemocyanin active sites;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1990-09

5. Folding of the polypeptide chain(s), conformational flexibility and reactivity of the metal active site of hemocyanin and tyrosinase;Biology of Metals;1990