Leslie Dutton

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Peter Leslie Dutton FRS is a British biochemist, and Eldridge Reeves Johnson Professor of Biochemistry and Biophysics in the Perelman School of Medicine at the University of Pennsylvania. [1] [2] He is a 2013 recipient of the John Scott Award for his work on electron transfer, studying the organization of electrons in cells and the mechanisms by which they convert light or oxygen into energy for the cell. [3]

Contents

Education

Leslie Dutton was born in England. He received a B.Sc. (Honors) in Chemistry at the University of Wales in 1963, and a Ph.D. in Biochemistry at the University of Wales in 1967. [4]

Research

In 1968, Leslie Dutton joined the University of Pennsylvania, [3] where he now leads the Dutton lab at the Perelman School of Medicine. [5] He is also Principal Investigator at the Photosynthetic Antenna Research Center. [6]

Dr. Dutton attempts to understand elementary processes of oxidation-reduction and related biological events. Natural enzymes called oxidoreductases are involved in biological functions including gene regulation, signalling, long range electron transfer, energy conversion (in photosynthesis and respiration), atom transport, drug detoxification, and enzyme catalysis. Using physical, chemical and computational methods, the Dutton lab studies oxidoreductases and redox proteins to discover mechanisms of electron transfer over large distances through proteins and understand quantum mechanical electron tunneling theory. Understanding electron tunnelling gives scientists a foundation for investigation of biological redox reactions and their relationship to chemical events such as proton exchange, protein conformation, and energy conversion. [1]

Through their understanding of such processes, Dutton and his lab have been able to manipulate electron transfer in structured highly simplified settings, and create man-made versions of proteins. Such maquettes, simple versions of their highly complex biological counterparts, enable researchers to model the minimal requirements for function. Futuristic applications could include creation of clean energy sources and prevention of genetic and age-related diseases. [3]

Awards and honors

Related Research Articles

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Biochemistry or biological chemistry, is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells, in turn relating greatly to the understanding of tissues and organs, as well as organism structure and function. Biochemistry is closely related to molecular biology, which is the study of the molecular mechanisms of biological phenomena.

Oxidative phosphorylation The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.

Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.

Respiratory complex I

Respiratory complex I, EC 7.1.1.2 is the first large protein complex of the respiratory chains of many organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and translocates protons across the inner mitochondrial membrane in eukaryotes or the plasma membrane of bacteria.

Protein disulfide-isomerase

Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum (ER) in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore the enzyme acts to catalyze protein folding.

In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

Thioredoxin

Thioredoxin is a class of small redox proteins known to be present in all organisms. It plays a role in many important biological processes, including redox signaling. In humans, thioredoxins are encoded by TXN and TXN2 genes. Loss-of-function mutation of either of the two human thioredoxin genes is lethal at the four-cell stage of the developing embryo. Although not entirely understood, thioredoxin is linked to medicine through their response to reactive oxygen species (ROS). In plants, thioredoxins regulate a spectrum of critical functions, ranging from photosynthesis to growth, flowering and the development and germination of seeds. Thioredoxins play a role in cell-to-cell communication.

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NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6, also known as complex I-B17, is a protein that in humans is encoded by the NDUFB6 gene. NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 6, is an accessory subunit of the NADH dehydrogenase (ubiquinone) complex, located in the mitochondrial inner membrane. It is also known as Complex I and is the largest of the five complexes of the electron transport chain.

NDUFA2

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NDUFB10

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 is an enzyme that in humans is encoded by the NDUFB10 gene. NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 10 is an accessory subunit of the NADH dehydrogenase (ubiquinone) complex, located in the mitochondrial inner membrane. It is also known as Complex I and is the largest of the five complexes of the electron transport chain.

NDUFB11 Protein-coding gene in the species Homo sapiens

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References

  1. 1 2 "P. Leslie Dutton, Ph.D." Department of Biochemistry and Biophysics. Retrieved 21 November 2013.
  2. 1 2 Kreeger, Karen. "Renaissance Biochemist". 15 November 2013. Penn Medicine News Blog. Retrieved 21 November 2013.
  3. 1 2 3 4 Vitez, Michael (21 November 2013). "3 Phila. medical men to be honored". Philadelphia Inquirer. Retrieved 21 November 2013.
  4. ↑ "Peter Leslie Dutton". Synthetic Biology for Learning and Doing (Conference). Retrieved 21 November 2013.
  5. ↑ "Peter Leslie Dutton". Perelman School of Medicine. Retrieved 21 November 2013.
  6. ↑ "P. Leslie Dutton, Principal Investigator". Washington University in St. Louis. Archived from the original on 4 October 2013. Retrieved 21 November 2013.
  7. ↑ "P. Leslie Dutton". Pennergy: The Penn Center for Energy Innovation. Retrieved 21 November 2013.
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