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

Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562
P Garcia, M Bruix, M Rico, S Ciofi-Baffoni, L Banci, MC Ramachandra Shastry, H Roder, T de Lumley Woodyear, CM Johnson, AR Fersht, PD Barker
Journal of Molecular Biology
(2004)
346
Design and Characterisation of an Artificial DNA‐Binding Cytochrome
DD Jones, PD Barker
Chembiochem
(2004)
5
A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system
JWA Allen, PD Barker, SJ Ferguson
The Journal of biological chemistry
(2003)
278
Designing redox metalloproteins from bottom-up and top-down perspectives.
PD Barker
Current Opinion in Structural Biology
(2003)
13
Solution structure and characterization of the heme chaperone CcmE.
F Arnesano, L Banci, PD Barker, I Bertini, A Rosato, XC Su, MS Viezzoli
Biochemistry
(2002)
41
Reduction of horse heart ferricytochrome c by bovine liver ferrocytochrome b5. Experimental and theoretical analysis.
LD Eltis, RG Herbert, PD Barker, AG Mauk, SH Northrup
Biochemistry
(2002)
30
pH-Linked conformational regulation of a metalloprotein oxidation-reduction equilibrium: electrochemical analysis of the alkaline form of cytochrome c
PD Barker, AG Mauk
Journal of the American Chemical Society
(2002)
114
Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome c
SP Rafferty, LL Pearce, PD Barker, JG Guillemette, CM Kay, M Smith, AG Mauk
Biochemistry
(2002)
29
Direct electrochemistry of protein-protein complexes involving cytochrome c, cytochrome b5, and plastocyanin
S Bagby, PD Barker, LH Guo, HA Hill
Biochemistry
(2002)
29
Proton titration curve of yeast iso-1-ferricytochrome c. Electrostatic and conformational effects of point mutations.
PD Barker, MR Mauk, AG Mauk
Biochemistry
(2002)
30

Telephone number

01223 763096

Email address