Fluoride ion as a nmr relaxation probe of paramagnetic metalloenzymes: the binding of fluoride to galactose oxidase

Beverly J. Marwedel; Robert J. Kurland; Daniel J. Kosman; Murray J. Ettinger

doi:10.1016/S0006-291X(75)80450-5

Fluoride ion as a nmr relaxation probe of paramagnetic metalloenzymes: the binding of fluoride to galactose oxidase

Beverly J. Marwedel
, Robert J. Kurland
, Daniel J. Kosman
, Murray J. Ettinger

Biochemistry

SUNY Buffalo

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

The use of fluoride ion, as a novel nuclear magnetic resonance relaxation probe of paramagnetic metalloenzymes, has been tested on galactose oxidase. The concentration dependence of the F^- longitudinal relaxation rates, R₁ = 1/T₁, and competition studies with CN demonstrate that F binds to the enzyme at or near the Cu²⁺ site with a binding constant of the order of 1 M^-1. Competition studies with galactose indicate that a ternary or higher order complex between enzyme, galactose and F^- is formed.

Original language	English
Pages (from-to)	773-779
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	63
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(75)80450-5
State	Published - Apr 7 1975

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title = "Fluoride ion as a nmr relaxation probe of paramagnetic metalloenzymes: the binding of fluoride to galactose oxidase",

abstract = "The use of fluoride ion, as a novel nuclear magnetic resonance relaxation probe of paramagnetic metalloenzymes, has been tested on galactose oxidase. The concentration dependence of the F- longitudinal relaxation rates, R1 = 1/T1, and competition studies with CN demonstrate that F binds to the enzyme at or near the Cu2+ site with a binding constant of the order of 1 M-1. Competition studies with galactose indicate that a ternary or higher order complex between enzyme, galactose and F- is formed.",

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AU - Marwedel, Beverly J.

AU - Kurland, Robert J.

AU - Kosman, Daniel J.

AU - Ettinger, Murray J.

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Y1 - 1975/4/7

N2 - The use of fluoride ion, as a novel nuclear magnetic resonance relaxation probe of paramagnetic metalloenzymes, has been tested on galactose oxidase. The concentration dependence of the F- longitudinal relaxation rates, R1 = 1/T1, and competition studies with CN demonstrate that F binds to the enzyme at or near the Cu2+ site with a binding constant of the order of 1 M-1. Competition studies with galactose indicate that a ternary or higher order complex between enzyme, galactose and F- is formed.

AB - The use of fluoride ion, as a novel nuclear magnetic resonance relaxation probe of paramagnetic metalloenzymes, has been tested on galactose oxidase. The concentration dependence of the F- longitudinal relaxation rates, R1 = 1/T1, and competition studies with CN demonstrate that F binds to the enzyme at or near the Cu2+ site with a binding constant of the order of 1 M-1. Competition studies with galactose indicate that a ternary or higher order complex between enzyme, galactose and F- is formed.

UR - https://www.scopus.com/pages/publications/0016669787

U2 - 10.1016/S0006-291X(75)80450-5

DO - 10.1016/S0006-291X(75)80450-5

M3 - Article

C2 - 1131263

AN - SCOPUS:0016669787

SN - 0006-291X

VL - 63

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Fluoride ion as a nmr relaxation probe of paramagnetic metalloenzymes: the binding of fluoride to galactose oxidase

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