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Oxidation of Phenols, Anilines, and Benzenethiols by Fungal Laccases: Correlation between Activity and Redox Potentials as Well as Halide Inhibition

Xu, Feng·1996·Biochemistry
DOI 10.1021/bi952971a
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Abstract

A comparative study has been performed with several fungal laccases for the oxidation of a series of phenols, anilines, and benzenethiols and for the inhibition by halides. The observed K(m) and kcat were correlated to the structure of substrate. The change in log (kcat/K(m)) was found to be proportional to the one-electron redox potential difference between laccase's type 1 copper site and substrate. This correlation indicated that the first electron transfer from substrate to laccase was governed by the "outersphere" mechanism. Compared to the electronic factor, the steric effect of small o-substituents (such as methyl and methoxy groups) was found to be unimportant. The depth of the laccase's type 1 copper site was estimated as approximately 10 A by comparing the steric effect among five 2-methoxyphenols whose 4-substituents ranged from 0.1 to 14 kDa in mass. The observed inhibition potency order of F- > Cl- > Br- was attributed to limited accessibility of laccase's type 2/type 3 trinuclear copper cluster site. Although the enzymes studied have homologous primary sequences and predicted similar backbone structures, the difference exhibited by each enzyme (in interacting with individual substrate or inhibitor) suggested the structural variation in their functional domains.

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Metadata

Authors
Xu, F.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1996-01-01
Volume
35
Issue
23
Pages
7608-7614
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi952971a
OpenAlex
W2010929717
Cited by
726
References
0
FWCI
13.55
Type
journal article
Language
en
Open access
closed

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