Volume 64, 1968
From the journal:

Transactions of the Faraday Society

Kinetics of complex formation of molybdate with 8-hydroxyquinoline. A model system for enzyme-substrate binding in xanthine oxidase

P. F. Knowles  and  H. Diebler  

Abstract

Using the temperature-jumps relaxation technique the kinetics of complex formation between molybdate and 8-hydroxyquinoline have been studied in the pH range 7.9–8.9. A reaction scheme for formation of the 1:1 complex is proposed which accounts for the observed pH dependence of the overall forward and backward rate constants. The specific rate constants evaluated are discussed in terms of the detailed reaction mechanism. Complex formation between molybdate and 8-hydroxyquinoline may be regarded as a model for the binding of substrate by the enzyme xanthine oxidase. This enzyme contains molybdenum which probably is involved in substrate binding. The experimental data are compatible with this hypothesis.

About
Cited by
Related
Download options Please wait...

Article information

DOI
https://doi.org/10.1039/TF9686400977
Article type
Paper

Trans. Faraday Soc., 1968,64, 977-985

Permissions

Request permissions

Kinetics of complex formation of molybdate with 8-hydroxyquinoline. A model system for enzyme-substrate binding in xanthine oxidase

P. F. Knowles and H. Diebler, Trans. Faraday Soc., 1968, 64, 977 DOI: 10.1039/TF9686400977

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements