On the role of a cuprous ion intermediate in the galactose oxidase reaction

Daniel J. Kosman; Robert D. Bereman; Murray J. Ettinger; Ronald S. Giordano

doi:10.1016/0006-291X(73)90772-9

On the role of a cuprous ion intermediate in the galactose oxidase reaction

Daniel J. Kosman
, Robert D. Bereman
, Murray J. Ettinger
, Ronald S. Giordano

Biochemistry

SUNY Buffalo

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

20 Scopus citations

Abstract

The Cu⁺² electron spin resonance spectrum of galactose oxidase (galactose:O₂ oxidoreductase, E.C. 1.1.3.9) indicates that the metal is in a pseudo-square planar environment. The electron g values are: g_zz = 2.273, g_xx = 2.058 and g_yy = 2.048. The copper nuclear hyperfine constants are (in Gauss): A_zz = 176.5, A_xx = 28.8 and A_yy = 30.1. This spectrum is unaltered in either intensity or g or A values under conditions which cause the inhibition of galactose oxidase by superoxide dismutase. No combination of substrates (galactose and O₂) and oxidant traps (superoxide dismutase and catalase) results in the reduction of the cupric ion resonance. Thus, a Cu⁺¹-enzyme does not appear to be a stable intermediate along this enzyme's reaction path.

Original language	English
Pages (from-to)	856-861
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	54
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(73)90772-9
State	Published - Oct 1 1973

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title = "On the role of a cuprous ion intermediate in the galactose oxidase reaction",

abstract = "The Cu+2 electron spin resonance spectrum of galactose oxidase (galactose:O2 oxidoreductase, E.C. 1.1.3.9) indicates that the metal is in a pseudo-square planar environment. The electron g values are: gzz = 2.273, gxx = 2.058 and gyy = 2.048. The copper nuclear hyperfine constants are (in Gauss): Azz = 176.5, Axx = 28.8 and Ayy = 30.1. This spectrum is unaltered in either intensity or g or A values under conditions which cause the inhibition of galactose oxidase by superoxide dismutase. No combination of substrates (galactose and O2) and oxidant traps (superoxide dismutase and catalase) results in the reduction of the cupric ion resonance. Thus, a Cu+1-enzyme does not appear to be a stable intermediate along this enzyme's reaction path.",

author = "Kosman, \{Daniel J.\} and Bereman, \{Robert D.\} and Ettinger, \{Murray J.\} and Giordano, \{Ronald S.\}",

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doi = "10.1016/0006-291X(73)90772-9",

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TY - JOUR

T1 - On the role of a cuprous ion intermediate in the galactose oxidase reaction

AU - Kosman, Daniel J.

AU - Bereman, Robert D.

AU - Ettinger, Murray J.

AU - Giordano, Ronald S.

PY - 1973/10/1

Y1 - 1973/10/1

N2 - The Cu+2 electron spin resonance spectrum of galactose oxidase (galactose:O2 oxidoreductase, E.C. 1.1.3.9) indicates that the metal is in a pseudo-square planar environment. The electron g values are: gzz = 2.273, gxx = 2.058 and gyy = 2.048. The copper nuclear hyperfine constants are (in Gauss): Azz = 176.5, Axx = 28.8 and Ayy = 30.1. This spectrum is unaltered in either intensity or g or A values under conditions which cause the inhibition of galactose oxidase by superoxide dismutase. No combination of substrates (galactose and O2) and oxidant traps (superoxide dismutase and catalase) results in the reduction of the cupric ion resonance. Thus, a Cu+1-enzyme does not appear to be a stable intermediate along this enzyme's reaction path.

AB - The Cu+2 electron spin resonance spectrum of galactose oxidase (galactose:O2 oxidoreductase, E.C. 1.1.3.9) indicates that the metal is in a pseudo-square planar environment. The electron g values are: gzz = 2.273, gxx = 2.058 and gyy = 2.048. The copper nuclear hyperfine constants are (in Gauss): Azz = 176.5, Axx = 28.8 and Ayy = 30.1. This spectrum is unaltered in either intensity or g or A values under conditions which cause the inhibition of galactose oxidase by superoxide dismutase. No combination of substrates (galactose and O2) and oxidant traps (superoxide dismutase and catalase) results in the reduction of the cupric ion resonance. Thus, a Cu+1-enzyme does not appear to be a stable intermediate along this enzyme's reaction path.

UR - https://www.scopus.com/pages/publications/0015807755

U2 - 10.1016/0006-291X(73)90772-9

DO - 10.1016/0006-291X(73)90772-9

M3 - Article

C2 - 4356659

AN - SCOPUS:0015807755

SN - 0006-291X

VL - 54

SP - 856

EP - 861

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

On the role of a cuprous ion intermediate in the galactose oxidase reaction

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