Steven K. Chapman

Chemistry University of Edinburgh, Edinburgh, Scotland, United Kingdom 
"Steven Chapman"
Mean distance: 39957


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James H. Naismith research assistant 1989-1989 Edinburgh
Bor-Ran Li grad student
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Efimov I, Basran J, Sun X, et al. (2012) The mechanism of substrate inhibition in human indoleamine 2,3-dioxygenase. Journal of the American Chemical Society. 134: 3034-41
Davydov RM, Chauhan N, Thackray SJ, et al. (2010) Probing the ternary complexes of indoleamine and tryptophan 2,3-dioxygenases by cryoreduction EPR and ENDOR spectroscopy. Journal of the American Chemical Society. 132: 5494-500
Mowat CG, Gazur B, Campbell LP, et al. (2010) Flavin-containing heme enzymes. Archives of Biochemistry and Biophysics. 493: 37-52
Chauhan N, Thackray SJ, Rafice SA, et al. (2009) Reassessment of the reaction mechanism in the heme dioxygenases. Journal of the American Chemical Society. 131: 4186-7
Pessanha M, Rothery EL, Miles CS, et al. (2009) Tuning of functional heme reduction potentials in Shewanella fumarate reductases Biochimica Et Biophysica Acta - Bioenergetics. 1787: 113-120
Thackray SJ, Mowat CG, Chapman SK. (2008) Exploring the mechanism of tryptophan 2,3-dioxygenase. Biochemical Society Transactions. 36: 1120-3
Paixão VB, Salgueiro CA, Brennan L, et al. (2008) The solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel family structural motif. Biochemistry. 47: 11973-80
Li BR, Anderson JL, Mowat CG, et al. (2008) Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity. Biochemical Society Transactions. 36: 992-5
Thackray SJ, Bruckmann C, Anderson JL, et al. (2008) Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding. Biochemistry. 47: 10677-84
De Laurentis W, Khim L, Anderson JL, et al. (2007) The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily. Biochemistry. 46: 12393-404
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