Steven K. Chapman
Affiliations: | Chemistry | University of Edinburgh, Edinburgh, Scotland, United Kingdom |
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"Steven Chapman"Mean distance: 39957
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Sign in to add trainee| James H. Naismith | research assistant | 1989-1989 | Edinburgh |
| Bor-Ran Li | grad student |
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Publications
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| 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 |
| Atkinson SJ, Mowat CG, Reid GA, et al. (2007) An octaheme c-type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine. Febs Letters. 581: 3805-8 |
| Forouhar F, Anderson JL, Mowat CG, et al. (2007) Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America. 104: 473-8 |