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Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase.

Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase. Research Abstract Details 

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  • Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase. Abstract Text:

    y kidaniY Kidani,j hiroseJ Hirose,h koikeH Koike,

    The mechanism of removal of the zinc ion from bovine carbonic anhydrase [EC 4.2.1.1] (BCA) by a chelating agent was studied. It was shown that the removal of the zinc ion from BCA took place through the formation of a ternary complex involving the enzyme, chelating agent, and metal ions. The formation constant of the ternary complex (KEML) was 10(2) M-1. This value was lower than the formation constant assumed by Wilkins. The reaction of zinc-2, 6-pyridinedicarboxylate complex with the apoenzyme also took place through the formation of the ternary complex and the species which reacted with apo-BCA was a 1:1 complex of zinc and 2, 6-pyridine-dicarboxylate. The theoretical equilibrium equation derived from the reaction mechanism showed a good fit with observed equilibrium dialysis data.

    Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase. Publishing Authors By Initials

    y kidaniY Kidani,j hiroseJ Hirose,h koikeH Koike,

    For similar inorganic chemicals: elements: metals, heavy: zinc research abstracts see: inorganic chemicals: elements: metals, heavy: zinc research

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    Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 79

    Page Numbers: 43-51

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jan

    YEAR: 1976

    Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase. Keywords Mesh Terms:

    KEYWORDS: Zinc

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase. Information

    Substance Name: Carbonic Anhydrases

    Registry Number: EC 4.2.1.1

    Grant and Affiliation Information for Coordination chemical studies on metalloenzymes. Kinetics and mechanism of the Zn(II) exchange reaction between chelating agent and apo-bovine carbonic anhydrase.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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