Reactivity of Haloperoxidases and Functional Mimics of Haloperoxidase
Abstract
The objective of the proposal was 1) to investigate oxidative coupling of nitro-toluene compounds, catalyzed by vanadium bromoperoxidase or its functional mimics and 2) to investigate catalytic properties of silicate-encapsulated enzymes, in general, and haloperoxidase enzymes, in particular, or their functional mimics to assess their utility as catalysts in relevant synthetic schemes. It was found that V-BrPO catalyzed bromination reactions with TNT do not effect the oxidative coupling reaction required to form FINS. FeHeme chloroperoxidase, which functions optimally at low pH is also not suitable for catalyzing the oxidative coupling of TNT to FINS because if only chlorinates at low pH. It was also found that haloperoxidases immobilized in mesoporous silicate matrices retain their catalytic and functional properties. These enzymes may well have applications as anti-biofouling catalysts.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 07, 2004
- Accession Number
- ADA424776
Entities
People
- Alison Butler
Organizations
- University of California, Santa Barbara