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P. LESLIE DUTTON, Ph.D.

Eldridge Reeves Johnson Professor of Biochemistry and Biophysics
Director, Johnson Foundation for Molecular Biophysics
Fellow of the Royal Society
Former Chair, Department of Biochemistry and Biophysics (1994-2008)

1005 Stellar-Chance Building
T: (215) 898-0991
F: (215) 573-2235
dutton@mail.med.upenn.edu

Ph.D. University of Wales (1967) Biochemistry

pubmed

DESCRIPTION OF RESEARCH INTERESTS:

Dr. Dutton strives to understand elementary processes of oxidation-reduction and diverse biological events coupled to it, and to define the thresholds of oxidative failure potentiating pathogenesis.

Thirty percent of the nature's enzymes are oxidoreductases. They cover a wide range of biological functions including gene regulation, signalling, long range electron transfer, energy conversion (in photosynthesis and respiration), atom transport, drug detoxification, and a wide range of enzyme catalysis. Using a battery of physical, chemical and computational methods applied to a variety of oxidoreductases and redox proteins, the Dutton lab focuses on how biology controls the direction and speed of electron transfer with high fidelity over large distances through proteins: that is, which parameters drawn from quantum mechanical electron tunneling theory have been selected to engineer oxidoreductases.

Understanding electron tunnelling provides the foundation to investigate how biological redox reactions are coupled to the chemical events of proton exchange, protein conformation central to chemical catalysis signal transduction, and energy conversion.

In parallel to these investigations, the lab is exploring the possibility of synthesizing much simpler versions of the highly complex biological counterparts -- maquettes, constructed to reveal the minimal requirements for function. Work is aimed at designing protein that will self-assemble to incorporate porphyrins, chlorophylls, iron sulfur clusters, flavins, and quinones singly or together into synthetic protein. The goal is to understand the engineering of natural oxidoreductases and related enzymes to reproduce their action. Examples are photosynthetic reaction centers, phototactic signalling proteins, cytochrome oxidase, myoglobin, cytochrome P450, superoxide dismutase, ferredoxin and classical dehydrogenases. This interest extends to membrane associated oxidoreductase enzymes operate as the nanometer scale electronic units of respiratory and photosynthetic electron transfer chains that separate charges across the intracytoplasmic membranes.

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