... understanding life in molecular detail

Dr Lars Jeuken

Bioinorganic chemistry; membrane biology; electron transfer; microbial fuel cells

We are interested in the catalytic mechanisms of oxidoreductases (metallo-enzymes), particularly those residing in the lipid membrane. We study these enzymes by designing novel experimental plateforms in which the metallo-enzymes are ‘interfaced’ with conducting materials that either donate or accept electrons that are part of the catalysed reaction.

Current major projects include:
  • Single-enzyme studies of proton-pumping enzymes
  • The catalytic mechanism of membrane-bound hydrogenase
  • (Industrial project with MedImmune) Phage display of membrane-proteins
  • Artificial photosynthesis, a bionanotechnology approach

Our aim is to to understand the catalytic mechanism of redox enzymes, in particular those involved in respiration (oxidoreductases). We have develop novel electrode materials that interact directly with redox enzymes, including redox enzymes that reside in the lipid membrane. Membrane-enzymes are more difficult to study due to their amphiphatic nature. Many enzymes are studied in detergent solutions or only hydrohilic subunits are used. However, the lipid membrane has an important influence on the proteins that reside in them and experimental techniques that do not include the membrane are thus limited. Important examples are enzymes that interact with the hydrophobic quinone pool (like ubiquinol oxidase). Other examples include the 'membrane-bound hydrogenase', where the majority of studies are performed on the two hydrophilic subunits, without the third transmembrane quinone-converting subunit.

In our study of oxidoreductase we ofter develop new tools. One important developement has been the membrane-modified electrodes, where conducting, metallic surfaces (the electrode) are covered with a single (planer) lipid bilayer or a single layer of proteoliposomes containing the oxidoreductase. Using electrochemistry, it is possible to exchange electrons between the metallic surface and the oxidoreductase, proving a handle to monitor the catalytic turn-over. The electrode materials, including the ''membrane-modified electrodes', are characterised with a broad spectrum of tools, including Quartz-Crystal Microballance with Dissipation (QCM-D) and Atomic Force Spectroscopy (AFM). Finally, by combining our electrochemical methods with fluorescent techniques, we aim to obtain information about processes normally not detected by electrochemistry, such as proton pumping across the lipid membrane.

For more information about our research and projects, please goto http://www.fbs.leeds.ac.uk/jeukengroup/index.php

Detailed research programme                  Close ▲

Reader in Biophysics
MSc (Utrecht) PhD (Leiden)
BBSRC David Phillips Fellowship (2002-2007); BBS Young Investigator Award (2006); ERC Starting Fellowship (2012-2016)

Postdoc (Oxford) 1999-2002

Garstang South 10.140
School of Biomedical Sciences
0113 343 3829

Selected Publications

  1. Heath, G.R., Li, M., Polignano, I.L., Richens, J.L., Catucci, G., O’Shea, P., Sadeghi, S.J., Gilardi, G., Butt, J.N. and Jeuken, L.J.C. (2016) Layer-by-Layer Assembly of Supported Lipid Bilayer Poly-L-Lysine Multilayers,Biomacromolecules17, 324-335. DOI:10.1021/acs.biomac.5b01434

  2. Li, M., Jørgensen, S.K., McMillan, D.G.G., Krzemi?ski, L., Daskalakis, N.N., Partanen, R.H., Tutkus, M., Tuma, R., Stamou, D., Hatzakis, N.S., Jeuken, L.J.C. (2015) Single enzyme experiments reveal a long-lifetime proton leak state in a heme-copper oxidase, J. Am. Chem. Soc.137, 6055-16063. DOI: 10.1021/jacs.5b08798

  3. Hwang, E.T., Sheikh, K. Orchard, K.L., Hojo, D, Radu, V., Lee, C.-Y., Ainsworth, E., Lockwood, C., Gross, M.A., Adschiri, T., Reisner, E., Butt, J.N. and Jeuken, L.J.C. (2015) A Decaheme Cytochrome as a Molecular Electron Conduit in Dye-Sensitized Photoanodes, Adv. Funct. Mater. 25, 2308-2315. DOI: 10.1002/adfm.201404541

  4. Radu, V., Frielingsdorf, S., Evans, S.D., Lenz, O., Jeuken, L.J.C. (2014) Enhanced Oxygen-Tolerance of the Full Heterotrimeric Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutrophaJ. Am. Chem. Soc.136, 8512-8515.DOI: 10.1021/ja503138p Spotlight:DOI: 10.1021/ja5060466