Associate Professor Stephen Bell
|Telephone||+61 8 8313 4822|
BA Chemistry (Oxon), 1995
DPhil Chemistry University of Oxford, 2000 (The use of active site mutants of cytochrome P450cam in chemical synthesis)
Post doctoral Research Assistant, University of Oxford 2000-2004 and 2006-2009
Junior Research Fellow, The Queen's College Oxford, 2007-2011
Inorganic Chemistry Lecturer, Brasenose College Oxford, 2008-2011
Lecturer Inorganic Chemistry, University of Adelaide 2012-2014
Senior Lecturer and ARC Future Fellow, University of Adelaide 2015 to date
Biological Chemistry, Molecular Biology, Enzymology
I teach (or have taught) on the following courses
Foundations of Chemistry IB: Redox chemistry and Periodicity
Foundations of Chemistry IA: Molecular Behaviour
Environmental and Analytical Chemistry II: Separation Techniques (Chromatography and MS)
Chem II B: Applications of Symmetry
Advanced Synthetic Methods: Metals in Synthesis
Medicinal and Biological III: Electron transfer in Biology
Chem III: Inorganic Reaction Mechanism
Genome mining and protein engineering of cytochrome P450 enzymes for biocatalysis
The cytochrome P450 superfamily of haem iron monooxygenases is found in virtually all living organisms. They catalyse the oxidation of numerous endogenous and exogenous organic compounds and perform vital functions such as the biosynthesis of steroids and antibiotics and oxidative detoxification of xenobiotics. These monooxygenase enzymes catalyse the insertion of one atom of atmospheric oxygen into a carbon hydrogen bond.
R–H + 2H+ + 2e– + O2
R–OH + H2O
The screening, engineering and directed evolution of cytochrome P450 enzymes for the oxidation of non-natural substrates holds great promise for biotechnological applications. In the lab we study these cytochrome P450 enzymes and their electron transfer partners for biocatalysis and organic synthesis applications. The ultimate goal is to develop these systems as biocatalysts for clean, sustainable, low energy oxidation processes in natural product synthesis and bioremediation of recalcitrant compounds.
We engineer cytochrome P450 enzymes to alter their function and identify new enzymes from metabolically diverse bacteria which are capable of binding and oxidising a wide range of organic compounds. For example we have recently isolated CYP enzymes that are capable of hydroxylating sesquiterpenoids, steroids, alkanes, polyaromatic hydrocarbons and substituted aromatics. We also identify new and engineer existing electron transfer partners (e.g. iron-sulphur ferredoxin proteins and flavoproteins) in order to improve the efficiency of the enzymes which is essential for scale-up of their activity. We also develop whole cell oxidation systems, which enable the easy screening, scale-up and production of oxygenated organic products. We aim to further optimise and scale-up these systems (in vitro and in vivo) using fermentor technology and bioprocess engineering to generate products on a large scale.
With collaborators we are undertaking crystallographic, electrochemical and EPR (electron paramagnetic resonance) studies of these cytochrome P450 enzymes and their electron transfer partners in order to gain a better understanding of different steps in the catalytic cycle and the protein-protein interactions in these systems.
The Australian Research Council are currently funding our research into P450 mechanism through a Discovery Project Grant (DP140103229) with Prof. James de Voss at the University of Queensland. My research into isolating and understanding novel P450 electron transfer partners is funded through an ARC Future Fellowship (FT140100355).
I also have a research interest in the role of zinc and copper binding metallothioneins in neurodegenerative diseases.
My group currently consists of 2 PhD Students, 4 M. Phil Students and 2 Honours students.
Potential research students are directed to the Adelaide Graduate Centre for information on admissions, applications and scholarship
Questions regarding typical research projects can be directed to Dr Bell.
a full list of publications can be found here
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Entry last updated: Friday, 25 Jan 2019
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