Inhibition of enzymes by metal ion-chelating reagents. Theory and new graphical methods of study.

The Biochemical journal ·Vol. 137 ·No. 1 ·1974-01-00 ·Pages 55-60

Bardsley WG, Childs RE

Abstract

1. The mechanism of inhibition of enzymes by metal ion-chelating reagents is discussed and equations derived. 2. Two distinct mechanisms are postulated and graphical methods are given for differentiating between them. 3. Where the metal ion is actually removed from the enzyme to form a co-ordination complex in solution, a procedure is described for obtaining the stability constant for metal-enzyme interaction, the number of metal ions involved and the stoicheiometry of metal ion-ligand interaction.

MeSH Terms

Binding Sites Chelating Agents/pharmacology Enzyme Inhibitors Evaluation Studies as Topic Kinetics Ligands Mathematics Metals Methods Models, Chemical Protein Binding

Chemicals

Chelating Agents Enzyme Inhibitors Ligands Metals

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Bardsley W G

Childs R E

References (7)

7 references, click to expand

Aspects of enzyme mechanisms studies by nuclear spin relazation induced by paramagnetic probes.
Adv Enzymol Relat Areas Mol Biol. 1970;33:1-70 PMID: 4916855
Analysis of metal-protein complexes.
Methods Biochem Anal. 1956;3:265-99 PMID: 13369166
Kinetic studies on the rôle of zinc and diphosphopyridine nucleotide in the activity of yeast alcohol dehydrogenase.
J Biol Chem. 1956 Jul;221(1):491-500 PMID: 13345837
The role of zinc in alcohol dehydrogenases. II. The kinetics of the instantaneous reversible inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.
J Biol Chem. 1958 May;232(1):453-64 PMID: 13549433
The role of zinc in alcohol dehydrogenases. III. The kinetics of a time-dependent inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.
J Biol Chem. 1958 May;232(1):465-74 PMID: 13549434
The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on thestructure of the yeast alcohol dehydrogenase molecule.
J Biol Chem. 1960 Nov;235:3188-92 PMID: 13750715
The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection.
Biochim Biophys Acta. 1963 Feb 12;67:188-96 PMID: 14021669

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1370055

Published

1974-01-00

Pages

55-60

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1166079

Subset

External Links

PubMed source DOI: 10.1042/bj1370055 PMC Full Text View journal details

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Inhibition of enzymes by metal ion-chelating reagents. Theory and new graphical methods of study.

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