Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives

Max Wynn; Gary Stevens; David B. Knaff; Robert A. Holwerda

doi:10.1016/0003-9861(83)90630-6

Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives

Max Wynn, Gary Stevens, David B. Knaff, Robert A. Holwerda

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

3 Scopus citations

Abstract

3,4-Dihydroxyphenylalanine (DOPA) is not a preferred substrate of Rhus vernicifera laccase, as rate constants for the anaerobic reduction of the type 1 cupric atom by l-DOPA (6.3 × 10¹ m^-1 s^-1), d-DOPA (2.6 × 10¹ m^-1 s^-1), and l-DOPA methyl ester (2.6 × 10¹ m^-1 s^-1) are considerably smaller than k₁(catechol) (7 × 10² m^-1 s^-1) and rate constants characteristic of numerous other nonphysiological organic substrates (25 °C, pH 7.0, I = 0.5 m). The reactions of DOPA derivatives with laccase are unique, however, in that a two-term rate law pertains: k_obsd = k₀ + k₁[phenol]; k₀(l-DOPA) = 7 × 10^-2 s^-1. The reactivities of other catechol derivatives (pyrogallol, gallic acid, and methyl gallate) with laccase type 1 copper were also examined.

Original language	English (US)
Pages (from-to)	662-666
Number of pages	5
Journal	Archives of Biochemistry and Biophysics
Volume	223
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(83)90630-6
State	Published - Jun 1983

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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@article{ebf026ec119940d3b78640f942a771ba,

title = "Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives",

abstract = "3,4-Dihydroxyphenylalanine (DOPA) is not a preferred substrate of Rhus vernicifera laccase, as rate constants for the anaerobic reduction of the type 1 cupric atom by l-DOPA (6.3 × 101 m-1 s-1), d-DOPA (2.6 × 101 m-1 s-1), and l-DOPA methyl ester (2.6 × 101 m-1 s-1) are considerably smaller than k1(catechol) (7 × 102 m-1 s-1) and rate constants characteristic of numerous other nonphysiological organic substrates (25 °C, pH 7.0, I = 0.5 m). The reactions of DOPA derivatives with laccase are unique, however, in that a two-term rate law pertains: kobsd = k0 + k1[phenol]; k0(l-DOPA) = 7 × 10-2 s-1. The reactivities of other catechol derivatives (pyrogallol, gallic acid, and methyl gallate) with laccase type 1 copper were also examined.",

author = "Max Wynn and Gary Stevens and Knaff, {David B.} and Holwerda, {Robert A.}",

note = "Funding Information: D.B.K. (Grant D-710) and R.A.H. (Grant D-735) thank the Robert A. Welch Foundation for their support of this research.",

year = "1983",

month = jun,

doi = "10.1016/0003-9861(83)90630-6",

language = "English (US)",

volume = "223",

pages = "662--666",

journal = "Archives of Biochemistry and Biophysics",

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T1 - Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives

AU - Wynn, Max

AU - Stevens, Gary

AU - Knaff, David B.

AU - Holwerda, Robert A.

N1 - Funding Information: D.B.K. (Grant D-710) and R.A.H. (Grant D-735) thank the Robert A. Welch Foundation for their support of this research.

PY - 1983/6

Y1 - 1983/6

N2 - 3,4-Dihydroxyphenylalanine (DOPA) is not a preferred substrate of Rhus vernicifera laccase, as rate constants for the anaerobic reduction of the type 1 cupric atom by l-DOPA (6.3 × 101 m-1 s-1), d-DOPA (2.6 × 101 m-1 s-1), and l-DOPA methyl ester (2.6 × 101 m-1 s-1) are considerably smaller than k1(catechol) (7 × 102 m-1 s-1) and rate constants characteristic of numerous other nonphysiological organic substrates (25 °C, pH 7.0, I = 0.5 m). The reactions of DOPA derivatives with laccase are unique, however, in that a two-term rate law pertains: kobsd = k0 + k1[phenol]; k0(l-DOPA) = 7 × 10-2 s-1. The reactivities of other catechol derivatives (pyrogallol, gallic acid, and methyl gallate) with laccase type 1 copper were also examined.

AB - 3,4-Dihydroxyphenylalanine (DOPA) is not a preferred substrate of Rhus vernicifera laccase, as rate constants for the anaerobic reduction of the type 1 cupric atom by l-DOPA (6.3 × 101 m-1 s-1), d-DOPA (2.6 × 101 m-1 s-1), and l-DOPA methyl ester (2.6 × 101 m-1 s-1) are considerably smaller than k1(catechol) (7 × 102 m-1 s-1) and rate constants characteristic of numerous other nonphysiological organic substrates (25 °C, pH 7.0, I = 0.5 m). The reactions of DOPA derivatives with laccase are unique, however, in that a two-term rate law pertains: kobsd = k0 + k1[phenol]; k0(l-DOPA) = 7 × 10-2 s-1. The reactivities of other catechol derivatives (pyrogallol, gallic acid, and methyl gallate) with laccase type 1 copper were also examined.

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Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives

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