University Associate Professor

Research in my group can be divided into two areas, although these share a common theme of engineering metal protein interactions in novel ways.

One goal is to engineer novel proteins and polypeptide based assemblies that can be used in molecular electronic devices and nanotechnology in general. This involves understanding, at a fundamental level, how metal cofactors, particularly heme, is delivered to proteins in vivo and, in the case of c-type cytochromes, how heme is covalently attached to protein. It also involves understanding how functional protein units can be assembled into larger nanoscale assemblies that gain function through the proximity of the constituent monomers.

The other goal is to explore the interaction of 4d and 5d transition metals with proteins, particularly as a possible route to finding novel medicinal compounds. Specifically, Ruthenium organometallic complexes have shown some potential as anti cancer compounds, but little is understood about how the chemistry of Ruthenium interacts with biomolecules.

Research Interests

  • Self Assembly of Proteins into functional materials
  • Heme protein assembly and heme chaperones
  • Electrochemistry of Proteins
  • Heavy metal complexes and ther interaction with Proteins

Watch Dr Barker discuss his research

Publications

Metal and redox selectivity of protoporphyrin binding to the heme chaperone CcmE†
EM Harvat, O Daltrop, F Sobott, M Moreau, PD Barker, JM Stevens, SJ Ferguson
Metallomics : integrated biometal science
(2011)
3
Aberrant attachment of heme to cytochrome by the Ccm system results in a cysteine persulfide linkage
EB Sawyer, E Stephens, SJ Ferguson, JWA Allen, PD Barker
Journal of the American Chemical Society
(2010)
132
Tuning heavy metal compounds for anti-tumor activity: is diversity the key to ruthenium's success?
SM Page, SR Boss, PD Barker
Future medicinal chemistry
(2009)
1
Interfacial redox processes of cytochrome b 562
P Zuo, T Albrecht, PD Barker, DH Murgida, P Hildebrandt
Physical chemistry chemical physics : PCCP
(2009)
11
Variant c-type cytochromes as probes of the substrate specificity of the E. coli cytochrome c maturation (Ccm) apparatus.
JWA Allen, EB Sawyer, ML Ginger, PD Barker, SJ Ferguson
Biochemical Journal
(2009)
419
Measurement of Amyloid Fibril Length Distributions by Inclusion of Rotational Motion in Solution NMR Diffusion Measurements
AJ Baldwin, SJ Anthony‐Cahill, TPJ Knowles, G Lippens, J Christodoulou, PD Barker, CM Dobson
Angewandte Chemie
(2008)
120
Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements.
AJ Baldwin, SJ Anthony-Cahill, TPJ Knowles, G Lippens, J Christodoulou, PD Barker, CM Dobson
Angew Chem Int Ed Engl
(2008)
47
Contribution of rotational diffusion to pulsed field gradient diffusion measurements.
AJ Baldwin, J Christodoulou, PD Barker, CM Dobson, G Lippens
Journal of Chemical Physics
(2007)
127
An induced-fit conformational change underlies the binding mechanism of the heme-transport Proteobacteria-protein HemS
M Paoli, S Schneider, K Sharp, P Barker
FASEB JOURNAL
(2007)
21
An Induced Fit Conformational Change Underlies the Binding Mechanism of the Heme Transport Proteobacteria-Protein HemS*
S Schneider, KH Sharp, PD Barker, M Paoli
J Biol Chem
(2006)
281

Telephone number

01223 763096

Email address