Dc. Goodwin et al., EVIDENCE FOR VERATRYL ALCOHOL AS A REDOX MEDIATOR IN LIGNIN PEROXIDASE-CATALYZED OXIDATION, Biochemistry, 34(15), 1995, pp. 5060-5065
We have examined the hypothesis that veratryl alcohol (VA) may act as
a redox mediator in Lignin peroxidase (LiP)-catalyzed oxidations. The
oxidation of chlorpromazine (CPZ) by this system was used to evaluate
this hypothesis. Chlorpromazine can be oxidized by one electron to for
m a stable cation radical (CPZ(.+)). This cation radical can be oxidiz
ed by another electron to the sulfoxide (CPZSO). These oxidation steps
are easily monitored, making CPZ a useful chemical to investigate red
ox mediation by VA. Lignin peroxidase oxidized CPZ to CPZ(.+) whether
or not VA was present. The inclusion of VA, however, stimulated CPZ ox
idation to CPZ(.+) and subsequent oxidation of CPZ(.+) to CPZSO. In th
e absence of VA, the initial rates of CPZ oxidation by LiP were CPZ co
ncentration-dependent. However, when saturating concentrations of VA w
ere added, the oxidation of CPZ and CPZ(.+) became independent of CPZ
concentration. When the oxidation of VA to veratryl aldehyde was conce
ntrations of CPZ produced a lag in veratryl aldehyde appearance propor
tional to the concentration of CPZ. Conversely, increasing concentrati
ons of VA never inhibited CPZ oxidation. Transient-state kinetic studi
es indicated that both VA and CPZ reduced the compound I and compound
II forms of LiP. However, when saturating concentrations of VA were ut
ilized, LiP turnover was independent of CPZ concentration. We suggest
these data demonstrate that VA may act as a redox mediator for the ind
irect oxidation of compounds by LiP.