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Professor Stephen Chapman
e-mail: s.k.chapman@ed.ac.uk tel: 0131 650 4760

Research Interests: electron transfer; metalloproteins; biocatalysis; protein engineering; enzymology; oxygen activation; cytochromes; flavoproteins.

Our current research projects are centered on determining the molecular mechanisms involved in electron transfer in flavin and metal-containing enzymes. This involves an interdisciplinary research team investigating the physiochemical properties of heme proteins. The group has a number of enzymes cloned and expressed and is successfully analysing their molecular properties using a combination of protein engineering with kinetic and spectroscopic techniques.

Tryptophan Dioxygenase

We have recently determined the high-resolution X-ray structure of Tryptophan Dioxygenase. The figure shows the active site of the enzyme with the heme group in red and the bound tryptophan in green.

Systems currently being analysed using a combination of protein engineering with kinetic and spectroscopic, electrochemical and structural techniques are described in detail at the following web site: http://www.chem.ed.ac.uk/chapman/

 

 

 

 

 

SELECTED RECENT PUBLICATIONS

  1. “Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase” F. Forouhar, J.L.R. Anderson, C.G. Mowat, S.M. Vorobiev, A. Hussain, M. Abashidze, C. Bruckmann, S.J. Thackray, J. Seetharaman, T. Tucker, R. Xiao, L-C. Ma, L. Zhao, T.B. Acton, G.T. Montelione, S.K. Chapman, and L. Tong, Proc.Natl.Acad.Sci.USA 2007, 104, 473-478.
  2. “An octaheme c-type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine” S.J. Atkinson, C.G. Mowat, G.A. Reid, and S.K. Chapman, FEBS.Letts. 2007, 581, 3805-3808.
  3. “The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily” W. De Laurentis, L. Khim, J.L.R. Anderson, A. Adam, R.S. Phillips, S.K. Chapman, K-H. van Pee and J.H. Naismith, Biochemistry, 2007, 46, 12393-12404.
  4. “Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding” S. J. Thackray, C. Bruckmann, J.L.R. Anderson, L. P. Campbell, R.Xiao, L. Zhao C.G. Mowat, F. Forouhar, L. Tong, and S.K. Chapman, Biochemistry, 2008, 47, 10677-10684.
  5. “Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity” B-R. Li, J.L.R. Anderson, C.G. Mowat, C.S. Miles, G.A. Reid and S.K. Chapman, Biochem.Soc.Trans., 2008, 36, 992-995.
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