Evidence for Veratryl Alcohol as a Redox Mediator in Lignin Peroxidase-Catalyzed Oxidation

• Published in: Biochemistry (Easton) 1995-04, Vol.34 (15), p.5060-5065
• Main Authors: Goodwin, Douglas C, Aust, Steven D, Grover, Thomas A
• Format: Article
• Language: English
• Subjects: Benzyl Alcohols - metabolism; Catalysis; Chlorpromazine - metabolism; Electrons; Kinetics; Models, Chemical; Oxidation-Reduction; Peroxidases - metabolism
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00015a017

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 form a stable cation radical (CPZ.+). This cation radical can be oxidized by another electron to the sulfoxide (CPZSO). These oxidation steps are easily monitored, making CPZ a useful chemical to investigate redox mediation by VA. Lignin peroxidase oxidized CPZ to CPZ.+ whether or not VA was present. The inclusion of VA, however, stimulated CPZ oxidation to CPZ.+ and subsequent oxidation of CPZ.+ to CPZSO. In the absence of VA, the initial rates of CPZ oxidation by LiP were CPZ concentration-dependent. However, when saturating concentrations of VA were added, the oxidation of CPZ and CPZ.+ became independent of CPZ concentration. When the oxidation of VA to veratryl aldehyde was examined, increasing concentrations of CPZ produced a lag in veratryl aldehyde appearance proportional to the concentration of CPZ. Conversely, increasing concentrations of VA never inhibited CPZ oxidation. Transient-state kinetic studies indicated that both VA and CPZ reduced the compound I and compound II forms of LiP. However, when saturating concentrations of VA were utilized, LiP turnover was independent of CPZ concentration. We suggest these data demonstrate that VA may act as a redox mediator for the indirect oxidation of compounds by LiP.