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

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
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
The C Terminus of Apocytochrome b 562 Undergoes Fast Motions and Slow Exchange among Ordered Conformations Resembling the Folded State †
N D'Amelio, AMJJ Bonvin, M Czisch, P Barker, R Kaptein
Biochemistry
(2002)
41
A further clue to understanding the mobility of mitochondrial yeast cytochrome c
PD Barker, I Bertini, R Del Conte, SJ Ferguson, P Hajieva, E Tomlinson, P Turano, MS Viezzoli
European journal of biochemistry
(2001)
268
15N Backbone Dynamics of Ferricytochrome b 562: Comparison with the Reduced Protein and the R98C Variant †
M Assfalg, L Banci, I Bertini, S Ciofi-Baffoni, PD Barker
Biochemistry
(2001)
40
Haem ligand switches in engineered DNA binding cytochromes.
PD Barker
JOURNAL OF INORGANIC BIOCHEMISTRY
(2001)
86
Chimeric cytochromes as novel transducers
PD Barker, DD Jones
BIOPHYS J
(2001)
80
Structural consequences of b- to c-type heme conversion in oxidized Escherichia coli cytochrome b562
F Arnesano, L Banci, I Bertini, S Ciofi-Baffoni, TL Woodyear, CM Johnson, PD Barker
Biochemistry
(2000)
39
Still a puzzle: why is haem covalently attached in c-type cytochromes?
PD Barker, SJ Ferguson
Structure
(1999)
7
Coupled oxidation of heme covalently attached to cytochrome b(562) yields a novel biliprotein
JK Rice, IM Fearnley, PD Barker
Biochemistry
(1999)
38

Telephone number

01223 763096

Email address