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 tranistion 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.
A cytochrome b(562) 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 - J Biol Chem (
2003)
278, 52075
(DOI:
10.1074/jbc.M307196200)
Designing redox metalloproteins from bottom-up and top-down perspectives.
PD Barker - Current Opinion in Structural Biology (
2003)
13, 490
(DOI:
10.1016/S0959-440X(03)00108-8)
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, 13587
(DOI:
10.1021/bi026362w)
The C terminus of apocytochrome b562 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, 5505
(DOI:
10.1021/bi011863n)
N-15 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-US (
2001)
40, 12761
(DOI:
10.1021/bi0101300)
Haem ligand switches in engineered DNA binding cytochromes.
PD Barker - J INORG BIOCHEM (2001) 86, 23
A further clue to understanding the mobility of mitochondrial yeast cytochrome c: a (15)N T1rho investigation of the oxidized and reduced species.
PD Barker, I Bertini, R Del Conte, SJ Ferguson, P Hajieva, E Tomlinson, P Turano, MS Viezzoli - Eur J Biochem (
2001)
268, 4468
(DOI:
10.1046/j.1432-1327.2001.02369.x)
Chimeric cytochromes as novel transducers
PD Barker, DD Jones - BIOPHYS J (2001) 80, 338A
Structural consequences of b- to c-type heme conversion in oxidized Escherichia coli cytochrome b(562)
F Arnesano, L Banci, I Bertini, S Ciofi-Baffoni, TD Woodyear, CM Johnson, PD Barker - Biochemistry (
2000)
39, 1499
(DOI:
10.1021/bi991831o)
Coupled oxidation of heme covalently attached to cytochrome b(562) yields a novel biliprotein
JK Rice, IM Fearnley, PD Barker - BIOCHEMISTRY-US (
1999)
38, 16847
(DOI:
10.1021/bi990880y)
