Dopamine-β-hydroxylase: Evidence for binuclear copper sites

Ninian J. Blackburn; Howard S. Mason; Peter F. Knowles

doi:10.1016/0006-291X(80)91611-3

Dopamine-β-hydroxylase: Evidence for binuclear copper sites

Ninian J. Blackburn, Howard S. Mason, Peter F. Knowles

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

24 Scopus citations

Abstract

Copper has been progressively removed from dopamine-β-hydroxylase by incubation with chelex resin. The relationship between the activity (A) and the copper/protein ratio (r) has been shown to be of the form A^⊥r² which implies that the enzyme catalysed reaction is second order with respect to protein bound copper. These results support a model for the catalytic mechanism involving binuclear copper sites rather than the four copper atoms in the enzyme acting independently.

Original language	English (US)
Pages (from-to)	1275-1281
Number of pages	7
Journal	Topics in Catalysis
Volume	95
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(80)91611-3
State	Published - 1980
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Biophysics
Molecular Biology

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10.1016/0006-291X(80)91611-3

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title = "Dopamine-β-hydroxylase: Evidence for binuclear copper sites",

abstract = "Copper has been progressively removed from dopamine-β-hydroxylase by incubation with chelex resin. The relationship between the activity (A) and the copper/protein ratio (r) has been shown to be of the form A⊥r2 which implies that the enzyme catalysed reaction is second order with respect to protein bound copper. These results support a model for the catalytic mechanism involving binuclear copper sites rather than the four copper atoms in the enzyme acting independently.",

author = "Blackburn, {Ninian J.} and Mason, {Howard S.} and Knowles, {Peter F.}",

year = "1980",

doi = "10.1016/0006-291X(80)91611-3",

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T2 - Evidence for binuclear copper sites

AU - Blackburn, Ninian J.

AU - Mason, Howard S.

AU - Knowles, Peter F.

PY - 1980

Y1 - 1980

N2 - Copper has been progressively removed from dopamine-β-hydroxylase by incubation with chelex resin. The relationship between the activity (A) and the copper/protein ratio (r) has been shown to be of the form A⊥r2 which implies that the enzyme catalysed reaction is second order with respect to protein bound copper. These results support a model for the catalytic mechanism involving binuclear copper sites rather than the four copper atoms in the enzyme acting independently.

AB - Copper has been progressively removed from dopamine-β-hydroxylase by incubation with chelex resin. The relationship between the activity (A) and the copper/protein ratio (r) has been shown to be of the form A⊥r2 which implies that the enzyme catalysed reaction is second order with respect to protein bound copper. These results support a model for the catalytic mechanism involving binuclear copper sites rather than the four copper atoms in the enzyme acting independently.

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U2 - 10.1016/0006-291X(80)91611-3

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JO - Topics in Catalysis

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ER -

Dopamine-β-hydroxylase: Evidence for binuclear copper sites

Abstract

ASJC Scopus subject areas

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