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 4d tranistion metals with proteins, particularly as a possible route to finding novel medicinal compounds. Particularly, Ruthenium organometallic complexes have shown some potential as anti cancer compounds, but little is understood about how the chemistry of Ruthenium interacts with biomolecules.
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 3, 363 (2011) (DOI:
10.1039/c0mt00085j)
Aberrant attachment of heme to cytochrome by the Ccm system results in a cysteine persulfide linkage.
EB Sawyer, E Stephens, SJ Ferguson, JW Allen, PD Barker -
Journal of the American Chemical Society 132, 4974 (2010) (DOI:
10.1021/ja908241v)
Tuning heavy metal compounds for anti-tumor activity: is diversity the key to ruthenium's success?
SM Page, SR Boss, PD Barker -
Future Med Chem 1, 541 (2009) (DOI:
10.4155/FMC.09.25)
Interfacial redox processes of cytochrome b(562)
P Zuo, T Albrecht, PD Barker, DH Murgida, P Hildebrandt -
Physical Chemistry Chemical Physics 11, 7430 (2009) (DOI:
10.1039/b904926f)
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 419, 177 (2009) (DOI:
10.1042/BJ20081999)
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 47, 3385 (2008) (DOI:
10.1002/anie.200703915)
Contribution of rotational diffusion to pulsed field gradient diffusion measurements.
AJ Baldwin, J Christodoulou, PD Barker, CM Dobson, G Lippens -
Journal of Chemical Physics 127, 114505 (2007) (DOI:
10.1063/1.2759211)
Macroscopic 2D networks self-assembled from nanometer-sized protein/DNA complexes.
M Manzanera, DJ Frankel, H Li, D Zhou, A Bruckbauer, P Kreutzmann, JM Blackburn, C Abell, T Rayment, D Klenerman, PD Barker -
Nano Lett 6, 365 (2006) (DOI:
10.1021/nl051599+)
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 281, 32606 (2006) (DOI:
10.1074/jbc.M607516200)
Cytochrome display on amyloid fibrils.
AJ Baldwin, R Bader, J Christodoulou, CE MacPhee, CM Dobson, PD Barker -
Journal of the American Chemical Society 128, 2162 (2006) (DOI:
10.1021/ja0565673)
