Folding of the polypeptide chain(s), conformational flexibility and reactivity of the metal active site of hemocyanin and tyrosinase-Reference-Cited by-同舟云学术

Folding of the polypeptide chain(s), conformational flexibility and reactivity of the metal active site of hemocyanin and tyrosinase

Published:1990 Issue:2 Volume:3 Page:93-97
ISSN:0933-5854
Container-title:Biology of Metals
language:en
Short-container-title:Biol Metals

Author:

Beltramini Mariano,Santamaria Meri,Salvato Benedetto,Lerche Konrad

Publisher

Springer Science and Business Media LLC

Subject

General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology,General Medicine,Metals and Alloys,General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology,Biomaterials

Link

http://link.springer.com/content/pdf/10.1007/BF01179512.pdf

Reference13 articles.

1. Beltramini M, Ricchelli F, Salvato B (1984a) The kinetics of the reaction ofOctopus vulgaris hemocyanin with cyanide. Its significance for the structure of the 11 S subunit of molluscan hemocyanin. Inorg Chim Acta 92:209?217

2. Beltramini M, Ricchelli F, Tallandini L, Salvato B (1984b) The reaction between cyanide and the hemocyanin ofCarcinus maenas: a kinetic study. Inorg Chim Acta 92:219?227

3. Beltramini M, Santamaria M, Salvato B (1988) Effects of anions, Ca2+, Mg2+ and aliphatic alcohols on the reaction of hemocyanin with cyanide. Arch Biochem Biophys 262:149?158

4. Giacometti G, di Muro P, Salvato B, Beltramini M (1988) The reaction ofOctopus vulgaris hemocyanin with exogenous ligands. Proposal of an allosteric model for the binding of cyanide and thiourea to the 11S subunit. Arch Biochem Biophys 266:539?547

5. Huber M, Lerch K (1986) Active site and protein structure of tyrosinase: comparison to hemocyanin. In Linzen B (ed) Invertebrate oxygen carrier. Springer Verlag, Berlin, pp 265?276

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