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.
Still a puzzle: Why is haem covalently attached in c-type cytochromes?
PD Barker, SJ Ferguson - Structure (
1999)
7, R281
(DOI:
10.1016/S0969-2126(00)88334-3)
The solution structure of oxidized Escherichia coli cytochrome b(562)
F Arnesano, L Banci, I Bertini, J Faraone-Mennella, A Rosato, PD Barker, AR Fersht - Biochemistry (
1999)
38, 8657
(DOI:
10.1021/bi982785f)
Verdoheme covalently attached to a modified cytochrome b562 protein: Towards the conversion of a cytochrome to a phytochrome.
JK Rice, PD Barker - BIOPHYS J (1999) 76, A421
N-epsilon,N-epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation
GR Moore, MC Cox, D Crowe, MJ Osborne, FI Rosell, J Bujons, PD Barker, MR Mauk, AG Mauk - BIOCHEMICAL JOURNAL (1998) 332, 439
Direct electrochemical studies of cytochromes b562
PD Barker, JL Butler, P deOliveira, HAO Hill, NI Hunt - Inorganica Chimica Acta (
1996)
252, 71
(DOI:
10.1016/S0020-1693(96)05299-1)
Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions
PD Barker, SMV Freund - Biochemistry (
1996)
35, 13627
(DOI:
10.1021/bi961128p)
Bis-methionine ligation to heme iron in mutants of cytochrome b(562) .1. Spectroscopic and electrochemical characterization of the electronic properties'
PD Barker, EP Nerou, MR Cheesman, AJ Thomson, P deOliveira, HAO Hill - Biochemistry (
1996)
35, 13618
(DOI:
10.1021/bi961127x)
CONVERSION OF CYTOCHROME B(562) TO C-TYPE CYTOCHROMES
PD BARKER, EP NEROU, SMV FREUND, IM FEARNLEY - Biochemistry (
1995)
34, 15191
(DOI:
10.1021/bi00046a027)
Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling.
JG GUILLEMETTE, PD BARKER, LD ELTIS, TP LO, M SMITH, GD BRAYER, AG MAUK - Biochimie (
1994)
76, 592
(DOI:
10.1016/0300-9084(94)90136-8)
Transmutation of a heme protein.
PD BARKER, JC FERRER, M MYLRAJAN, TM LOEHR, R FENG, Y KONISHI, WD FUNK, RTA MACGILLIVRAY, AG MAUK - Proceedings of the National Academy of Sciences of the United States of America (
1993)
90, 6542
(DOI:
10.1073/pnas.90.14.6542)
