The binding of zinc(II) to Mung Bean Nuclease. A voltammetric study

Binding of zinc to Mung Bean Nuclease was investigated by anodic stripping voltammetry and cyclic voltammetry. These methods rely on the direct monitoring of the oxidation current of zinc in the absence and presence of Mung Bean Nuclease. Titration curves of Zn 2+ with the enzyme were obtained in co...

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Bibliographic Details
Published in:Journal of inorganic biochemistry 2003-04, Vol.94 (4), p.365-371
Main Authors: Pires de Castro, Clarissa Silva, Rodrigues SouzaDe, Jurandir, Bloch Júnior, Carlos
Format: Article
Language:English
Subjects:
Anodic stripping voltammetry
Binding Sites
Cations, Divalent
Cyclic voltammetry
Electrochemistry - methods
Kinetics
Models, Molecular
Mung Bean Nuclease
Oxidation-Reduction
Protein Binding
Single-Strand Specific DNA and RNA Endonucleases - metabolism
Titrimetry - methods
Zinc
Zinc - chemistry
Zinc - metabolism
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Summary:Binding of zinc to Mung Bean Nuclease was investigated by anodic stripping voltammetry and cyclic voltammetry. These methods rely on the direct monitoring of the oxidation current of zinc in the absence and presence of Mung Bean Nuclease. Titration curves of Zn 2+ with the enzyme were obtained in concentrations ranging from 1.08×10 −9 to 1.07×10 −8 M and 1.16×10 −8 to 1.04×10 −7 M. The acquired data were used to calculate the dissociation constant and the stoichiometry of the complex. The binding sites of zinc in the Mung Bean Nuclease molecule were investigated using cyclic voltammetry. Two types of binding sites for zinc were identified and were attributed to a mononuclear exposed zinc-binding site with catalytic function and to an inaccessible binuclear zinc-binding site with structural functions.
ISSN:0162-0134
1873-3344
DOI:10.1016/S0162-0134(03)00030-8