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Title: Identical linkage and cooperativity of oxygen and carbon monoxide binding to Octopus dofleini hemocyanin

Abstract

Employment of high-precision thin-layer methods has enabled detailed functional characterization of oxygen and carbon monoxide binding for (1) the fully assembled form with 70 binding sites and (2) the isolated chains with 7 binding sites of octopus dofleini hemocyanin. The striking difference in the cooperativities of the two ligands for the assembled decamer is revealed through an examination of the binding capacities and the partition coefficient, determined as functions of the activities of both ligands. A global analysis of the data sets supported by a two-state allosteric model assuming an allosteric unit of 7. Higher level allosteric interactions were not indicated. This contrasts to results obtained for arthropod hemocyanins. Oxygen and carbon monoxide experiments performed on the isolated subunit chain confirmed the presence of functional heterogeneity reported previously. The analysis shows two types of binding sites in the ratio of 4:3.

Authors:
; ; ; ;  [1]
  1. (Univ. of Colorado, Boulder (USA))
Publication Date:
OSTI Identifier:
5712258
Resource Type:
Journal Article
Journal Name:
Biochemistry; (USA)
Additional Journal Information:
Journal Volume: 28:4; Journal ID: ISSN 0006-2960
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; CARBON MONOXIDE; CROSS-LINKING; HEMOCYANIN; BIOCHEMISTRY; LIGANDS; MATHEMATICAL MODELS; MOLLUSCS; OXYGEN; PH VALUE; THIN-LAYER CHROMATOGRAPHY; ANIMALS; AQUATIC ORGANISMS; CARBON COMPOUNDS; CARBON OXIDES; CHALCOGENIDES; CHEMICAL REACTIONS; CHEMISTRY; CHROMATOGRAPHY; ELEMENTS; INVERTEBRATES; METALLOPROTEINS; NONMETALS; ORGANIC COMPOUNDS; OXIDES; OXYGEN COMPOUNDS; POLYMERIZATION; PROTEINS; SEPARATION PROCESSES; 560300* - Chemicals Metabolism & Toxicology

Citation Formats

Connelly, P.R., Gill, S.J., Miller, K.I., Zhou, G., and van Holde, K.E. Identical linkage and cooperativity of oxygen and carbon monoxide binding to Octopus dofleini hemocyanin. United States: N. p., 1989. Web. doi:10.1021/bi00430a061.
Connelly, P.R., Gill, S.J., Miller, K.I., Zhou, G., & van Holde, K.E. Identical linkage and cooperativity of oxygen and carbon monoxide binding to Octopus dofleini hemocyanin. United States. doi:10.1021/bi00430a061.
Connelly, P.R., Gill, S.J., Miller, K.I., Zhou, G., and van Holde, K.E. Tue . "Identical linkage and cooperativity of oxygen and carbon monoxide binding to Octopus dofleini hemocyanin". United States. doi:10.1021/bi00430a061.
@article{osti_5712258,
title = {Identical linkage and cooperativity of oxygen and carbon monoxide binding to Octopus dofleini hemocyanin},
author = {Connelly, P.R. and Gill, S.J. and Miller, K.I. and Zhou, G. and van Holde, K.E.},
abstractNote = {Employment of high-precision thin-layer methods has enabled detailed functional characterization of oxygen and carbon monoxide binding for (1) the fully assembled form with 70 binding sites and (2) the isolated chains with 7 binding sites of octopus dofleini hemocyanin. The striking difference in the cooperativities of the two ligands for the assembled decamer is revealed through an examination of the binding capacities and the partition coefficient, determined as functions of the activities of both ligands. A global analysis of the data sets supported by a two-state allosteric model assuming an allosteric unit of 7. Higher level allosteric interactions were not indicated. This contrasts to results obtained for arthropod hemocyanins. Oxygen and carbon monoxide experiments performed on the isolated subunit chain confirmed the presence of functional heterogeneity reported previously. The analysis shows two types of binding sites in the ratio of 4:3.},
doi = {10.1021/bi00430a061},
journal = {Biochemistry; (USA)},
issn = {0006-2960},
number = ,
volume = 28:4,
place = {United States},
year = {1989},
month = {2}
}