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 journalArticle

3 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)662-666
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume223
Issue number2
DOIs
StatePublished - 1983

Fingerprint

Laccase
Dihydroxyphenylalanine
Copper
Derivatives
Rate constants
Rhus
Pyrogallol
Gallic Acid
Substrates
Phenol
catechol
Esters
Atoms

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives. / Wynn, Max; Stevens, Gary; Knaff, David B.; Holwerda, Robert A.

In: Archives of Biochemistry and Biophysics, Vol. 223, No. 2, 1983, p. 662-666.

Research output: Contribution to journalArticle

Wynn, Max ; Stevens, Gary ; Knaff, David B. ; Holwerda, Robert A. / Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives. In: Archives of Biochemistry and Biophysics. 1983 ; Vol. 223, No. 2. pp. 662-666.
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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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