Enantioselective epoxidation catalyzed by manganese-substituted human carbonic anhydrase
type: CreativeWork
description: Artificial metalloenzymes are an important class of hybrid catalysts for enantioselective, regioselective and chemoselective organic transformations. Despite several limitations associated with this type of hybrid catalysts system and their limited development relative to small molecule catalysts, significant advances have been achieved over the past few decades. This thesis describes the background, applicability of such hybrid catalysts, anchoring strategies and methods involved in the improvement of catalytic activities of artificial metalloenzymes. The generation of a thermostable human carbonic anhydrase mutant, activity determination, generation of an artificial metalloenzyme (manganese-substituted human carbonic anhydrase) and its use as a catalyst for enantioselective epoxidation of olefins is also described.
abstract: Artificial metalloenzymes are an important class of hybrid catalysts for enantioselective, regioselective and chemoselective organic transformations. Despite several limitations associated with this type of hybrid catalysts system and their limited development relative to small molecule catalysts, significant advances have been achieved over the past few decades. This thesis describes the background, applicability of such hybrid catalysts, anchoring strategies and methods involved in the improvement of catalytic activities of artificial metalloenzymes. The generation of a thermostable human carbonic anhydrase mutant, activity determination, generation of an artificial metalloenzyme (manganese-substituted human carbonic anhydrase) and its use as a catalyst for enantioselective epoxidation of olefins is also described.
author: Weerasekara, Sagarika
language: en
date published: 2015-01-01
date modified: 2026-07-24T02:38:57Z
provider: Iowa State University
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Iowa State University

PropertyValue
property ID: DOI
value: 10.31274/etd-180810-4498