Enantioselective epoxidation catalyzed by manganese-substituted human carbonic anhydrase

Thumbnail Image
Date
2015-01-01
Authors
Weerasekara, Sagarika
Major Professor
Advisor
Levi M. Stanley
Committee Member
Journal Title
Journal ISSN
Volume Title
Publisher
Altmetrics
Authors
Research Projects
Organizational Units
Organizational Unit
Chemistry

The Department of Chemistry seeks to provide students with a foundation in the fundamentals and application of chemical theories and processes of the lab. Thus prepared they me pursue careers as teachers, industry supervisors, or research chemists in a variety of domains (governmental, academic, etc).

History
The Department of Chemistry was founded in 1880.

Dates of Existence
1880-present

Related Units

Journal Issue
Is Version Of
Versions
Series
Department
Chemistry
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.

Comments
Description
Keywords
Citation
Source
Subject Categories
Copyright
Thu Jan 01 00:00:00 UTC 2015