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Yusuf Hamied Department of Chemistry

 

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

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
– Eur J Biochem
(2001)
268,
4468
15N backbone dynamics of ferricytochrome b562:: Comparison with the reduced protein and the R98C variant
M Assfalg, L Banci, I Bertini, S Ciofi-Baffoni, PD Barker
– Biochemistry
(2001)
40,
12761
Haem ligand switches in engineered DNA binding cytochromes.
PD Barker
– J INORG BIOCHEM
(2001)
86,
23
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, TL Woodyear, CM Johnson, PD Barker
– Biochemistry
(2000)
39,
1499
Still a puzzle:: why is haem covalently attached in c-type cytochromes?
PD Barker, SJ Ferguson
– Structure
(1999)
7,
r281
Coupled oxidation of heme covalently attached to cytochrome b562 yields a novel biliprotein
JK Rice, IM Fearnley, PD Barker
– Biochemistry
(1999)
38,
16847
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
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
– Biochem J
(1998)
332 ( Pt 2),
439
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Research Group

Research Interest Groups

Telephone number

01223 763096

Email address

pdb30@cam.ac.uk