The Marsh Laboratory
Department of Chemistry • University of Michigan
Coenzyme B12
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Home | People | Publications | Research Projects | Glutamate mutase | Benzylsuccinate Synthase | Fluorous Proteins
Free radicals are usually considered highly reactive and harmful to cells. How do enzymes generate such reactive species and harness them to catalyze vital biological reactions?
A radical approach to catalysis:
the mechanism of B12 enzymes
Research Projects
Toluene is a persistent environmental contaminant of ground water, where a lack of oxygen makes it particularly hard to detoxify. Remarkably, some anaerobic bacteria can grow on toluene as their sole carbon source. To do this they use a radical enzyme called benzylsuccinate synthase.
Toluene degradation:
the mechanism of benzylsuccinate synthase
A de novo designed protein with a fluorocarbon core
The Marsh Laboratory
Department of Chemistry • University of Michigan
Thauera aromatica enjoying an aromatic meal!
Towards the non-stick egg
Designing fluorous proteins
Fluorocarbons have many novel and useful properties, e.g. chemically inert and non-sticky. Can we introduce some of the Teflon®-like properties of fluorocarbons into proteins by incorporating extensively fluorinated amino acids into their structures?
Glutamate Mutase
Benzylsuccinate synthase
Fluorous Proteins
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Our laboratory focuses on two areas of chemical biology. In one area, we seek to understand the remarkable catalytic prowess of enzymes, in particular those that use free radicals in catalysis. In the other area we are exploring the potential for developing novel biological catalysts and therapeutic agents offered by the de-novo design and synthesis of novel proteins incorporating highly fluorinated amino acids. Our research is inherently inter-disciplinary in nature and draws on a synergistic combination of bio-organic, bio-inorganic and bio-physical chemistry. |