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

Journal Article · Tue Feb 21 00:00:00 EST 1989 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00430a061· OSTI ID:5712258

Connelly, P R; Gill, S J; Miller, K I; Zhou, G; van Holde, K E ^[1]

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1. Univ. of Colorado, Boulder (USA)

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.

• OSTI ID: 5712258
• Journal Information: Biochemistry; (USA), Vol. 28:4; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

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