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Dr Ben Berks PDF Print
Dr Ben Berks, Tutor in BiochemistryReader in Biochemistry
Tutor in Biochemistry

Office Phone
:  01865 613294 (internal 13294)
Lab Office Phone: 01865 613311    (internal 13311)
Lab Phone: 01865 613312   (internal 13312)
Fax: 01865 613201
E-mail: ben.berks@bioch.ox.ac.uk

Research Interests
Protein transport: Compartmentalisation of the cell by means of sealed membrane systems is a fundamental feature of cellular life. As a consequence a large proportion of newly-synthesised proteins must be transported across membranes to reach their correct destinations. We have discovered, and are now studying, a mechanistically unusual bacterial protein export pathway called Tat. The Tat system is involved in a wide range of fundamental cellular processes including energy metabolism, cell division, motility, bacterial pathogenesis, symbiotic nitrogen fixation, and quorum sensing. The most remarkable feature of the Tat system is that the substrate proteins are transported in a folded state. The Tat transporter therefore faces the formidable challenge of moving structured macromolecular substrates across a membrane without compromising the permeability barrier of the membrane to small molecules and ions. Working with the model organism Escherichia coli our studies are concentrated on determining the structure and mechanism of the Tat transporter.
Sulfur oxidation: We are undertaking structure-led studies into the molecular basis of the oxidation of inorganic sulfur compounds by bacteria.This is an ancient and widespread metabolism that provides the reductant for carbon dioxide fixation in many autotrophic organisms and is a major driver of the biogeochemical Sulfur Cycle. A wide variety of chemical reactions are required to complete the transformations and so the enzymes of the pathway provide a range of interesting mechanisms to study.
Biogenesis of Nitrous Oxide Reductase: This enzyme carries out the chemically very challenging task of breaking down the potent greenhouse gas nitrous oxide. The active site of the enzyme is an unprecedented copper-sulfide cluster. We are trying to understand the complex biosynthetic pathway by which this unusual cluster is assembled.
Other interests: Structural biology of membrane proteins, bacterial energy metabolism, bacterial cell biology.
Techniques: We utilise the full range of modern molecular techniques including protein biochemistry, molecular genetics, spectroscopic and biophysical methods including single molecule approaches, together with structure determination by X-ray diffraction and other techniques.

Links
Dr Berks' Departmental Webpage