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Chris Kay | London Centre for Nanotechnology

Prof Chris Kay

tel: +44 (0)207 679 7312
ext: 37312
fax: +44 (0)207 679 7096
office:

Structural & Molecular Biology

Research interests:

Characterisation of defects and dopants in semiconductors such as diamond and silicon
Structure and function studies of redox active proteins, including flavoproteins, quinoproteins, and metalloproteins
Characterisation of novel materials based on derivatives of porphyrins and phthalocyanines
Combining X-ray crystallography with nitroxide spin-labelling to build models of proteins in their working states

Biography:

  • DPhil, Department of Physical Chemistry, Oxford University 1990 – 1993
  • Postdoctoral Fellow, Department of Physics, Free University Berlin 1993 – 1997
  • Research Scientist, Department of Physics, Free University Berlin 1997 – 2005
  • Senior Lecturer, Department of Biology, University College London 2006 – 2011
  • Reader in EPR Spectroscopy, Research Department of Structural and Molecular Biology, University College London 2011 – 2014
  • Professor of EPR Spectroscopy, Research Department of Structural and Molecular Biology, University College London 2014 - present
Awards and honours: 

Royal Society of Chemistry, Fellow

Higher Education Academy, Associate Fellow

External positions held: 
  • Secretary, ESR Spectroscopy Group of the RSC (2006-11)
  •  
Memberships : 

American Chemical Society

International EPR Society

Research: 

ESR/EPR can provide unique information on the identity and structure of stable and transient paramagnetic species such as defects, metals, clusters and organic cofactors, and nitroxide spin-labels engineered into proteins by, for example, ENDOR (electron-nuclear double resonance) and HYSCORE (hyperfine correlation spectroscopy). In addition, pulsed ELDOR (electron-electron double resonance) can measure distances between electron spins over the range 15 – 80 Å. Furthermore, the time-domain on the nanosecond scale can be accessed by initiation of reactions using a laser pulse that simultaneously triggers detection by pulsed EPR.

Recent publications

  • "Structure of the Pyrroloquinoline Quinone Radical in Quinoprotein Ethanol Dehydrogenase" [PDF File] C. W. M. Kay, B. Mennenga, H. Görisch, and R. Bittl. Journal of Biological Chemistry 281 (2006) 1470-1476.
  • "Substrate binding in quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa studied by electron-nuclear double resonance" [PDF File] C. W. M. Kay, B. Mennenga, H. Görisch and R. Bittl. Proc Natl Acad Sci (USA) 2006 (103) 5267-5272.

A number of Gram-negative bacteria utilize a class of dehydrogenases known as quinoproteins, which are distinct from the flavin- and nicotinamide-dependent enzymes, to catalyze the oxidation of alcohols or aldoses. The reaction is the first step in an electron transport chain that generates a proton motive force that is used to produce ATP. Several quinoproteins contain the noncovalently bound quinoid cofactor pyrroloquinoline quinone (PQQ), the role of which as a potential vitamin in mammals is currently under debate. The first of these papers describes the characterisation of the PQQ radical in Quinoprotein Ethanol Dehydrogenase, by advanced EPR & density functional theory. Although the structure of these proteins has been elucidated by X-ray crystallography until now the location of the alcohol substate could not be determined. In the second of these papers we established the position of the substrate in the binding pocket using the same experimental and theoretical methods.

Serum transferrin and lactoferrin are members of an important group of iron-binding and transport proteins.A single polypeptide folds into two lobes of similar structure, each binding a single Fe3+ ion. The iron can be removed and replaced by a number of other metal ions, while retaining the overall protein structure. Of great interest is how these proteins interact with their bacterial and mammalian receptors and how changes to the tertiary structure upon binding ultimately lead to iron release. In this paper, we measured the distance between the metal centers in copper-containing transferrin and lactoferrin by pulsed ELDOR. This work lays the basis for using EPR to directly observe changes in conformation in these proteins, and in other metalloproteins using the intrinsic metal centers as spin-labels, rather than having to artificially label them.

  • "Blue light perception in plants. Detection and characterization of a light-induced neutral flavin radical in a C450A mutant of phototropin" [PDF File] C. W. M. Kay, E. Schleicher, A. Kuppig, H. Hofner, W. Rüdiger, M. Schleicher, M. Fischer, A. Bacher, S. Weber, G. Richter J Biol Chem 278 (2003) 10973-10982

Numerous phenomena in the life cycle of plants such as circadian timing, regulation of gene expression, and phototropism (theadaptive process whereby plants bend toward a light source tomaximize light capture for photosynthesis) are responses to ambientlight levels in the UV-A and blue spectral regions comprisingwavelengths of about 320-500 nm. Up to the present, two classesof blue light photoreceptors have been identified in plants; theyare the cryptochromes and the phototropins,both of which are flavoproteins. In this paper we investigated the photoactivity of phototropins by advanced EPR spectroscopic methods and based on the results could suggest a radical pair mechanism as the basis for the formation of the intermediate signaling state, a covalent adduct between the flavin cofactor and nearby cysteine residue.

Research Highlights

Magnetism in a molecular thin film traditionally used in plastic electronics survives at temperatures reaching up to 100K,...
Phthalocyanine thin film on a flexible plastic substrate
A common blue pigment could have an important role to play in the development of a quantum computer, according to a paper...
EPR-derived model showing the dynamics of the pore and C-terminal domain
A major step forward in understanding how sodium channels function has been made by a team of researchers at the...
X-ray structure of RImN from Escherichia coli in complex with S-adenosyllmetioni
Researchers at the London Centre of Nanotechnology and Universities of Bristol and Southampton have made a crucial step...
The complex formed between the antibody fragment with the label (green and yello
A new biosensing assay which can specifically and rapidly detect colorectal cancer biomarkers in solution has been developed...
Novel flexible, lightweight and low cost “plastic” electronics, including OLEDs and organic solar cells, rely on...
New research has demonstrated a way to make bismuth electrons and nuclei work together as qubits in a quantum computer. The...
The ability of bacteria to cause diseases depends, among other things, on their ability to stick to their host in order to...
Teaching: 
  • Lecturing at undergraduate and postgraduate levels
  • Teaching of a postgraduate laboratory course
  • Supervising undergraduate and postgraduate research projects