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

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
Journal of Biological Chemistry
(2003)
278
Designing redox metalloproteins from bottom-up and top-down perspectives.
PD Barker
Curr Opin Struct Biol
(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
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
Conversion of Cytochrome b562 to c-Type Cytochromes
PD Barker, EP Nerou, SM Freund, IM Fearnley
Biochemistry
(2002)
34
EFFECTS OF CHARGED AMINO-ACID MUTATIONS ON THE BIMOLECULAR KINETICS OF REDUCTION OF YEAST ISO-1-FERRICYTOCHROME-C BY BOVINE FERROCYTOCHROME-B(5)
SH Northrup, KA Thomasson, CM Miller, PD Barker, LD Eltis, JG Guillemette, SC Inglis, AG Mauk
Biochemistry
(2002)
32
Proton linkage of complex formation between cytochrome c and cytochrome b5: electrostatic consequences of protein-protein interactions.
MR Mauk, PD Barker, AG Mauk
Biochemistry
(2002)
30
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
Direct Electrochemistry of Protein-Protein Complexes Involving Cytochrome c, Cytochrome b5, and Plastocyanin
S Bagby, PD Barker, LH Guo, HA Hill
Biochemistry
(2002)
29

Telephone number

01223 763096

Email address