Zobrazeno 1 - 10
of 194
pro vyhledávání: '"Stephen K Chapman"'
Autor:
J. L. Ross Anderson, Stephen K Chapman, Sarah J. Thackray, Emma Lloyd Raven, Christopher G. Mowat, Roman Davydov, Nishma Chauhan, Brian M. Hoffman, Nektaria D. Papadopoulou
Publikováno v:
Journal of the American Chemical Society
Davydov, R M, Chauhan, N, Thackray, S J, Anderson, J L R, Papadopoulou, N D, Mowat, C G, Chapman, S K, Raven, E L & Hoffman, B M 2010, ' Probing the Ternary Complexes of Indoleamine and Tryptophan 2,3-Dioxygenases by Cryoreduction EPR and ENDOR Spectroscopy ', Journal of the American Chemical Society, vol. 132, no. 15, pp. 5494-5500 . https://doi.org/10.1021/ja100518z
Davydov, R M, Chauhan, N, Thackray, S J, Anderson, J L R, Papadopoulou, N D, Mowat, C G, Chapman, S K, Raven, E L & Hoffman, B M 2010, ' Probing the Ternary Complexes of Indoleamine and Tryptophan 2,3-Dioxygenases by Cryoreduction EPR and ENDOR Spectroscopy ', Journal of the American Chemical Society, vol. 132, no. 15, pp. 5494-5500 . https://doi.org/10.1021/ja100518z
We have applied cryoreduction/EPR/ENDOR techniques to characterize the active-site structure of the ferrous-oxy complexes of human (hIDO) and Shewanella oneidensis (sIDO) indoleamine 2,3-dioxygenases, Xanthomonas campestris (XcTDO) tryptophan 2,3-dio
Publikováno v:
Archives of Biochemistry and Biophysics. 493:37-52
There are many examples of oxidative enzymes containing both flavin and heme prosthetic groups that carry out the oxidation of their substrate. For the purpose of this article we have chosen five systems. Two of these, the L-lactate dehydrogenase fla
Autor:
Caroline S Miles, Miguel Pessanha, Stephen K Chapman, Ricardo O. Louro, Graeme A Reid, David L. Turner, Emma L Rothery, Carlos A. Salgueiro, António V. Xavier
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1787(2):113-120
The fumarate reductases from S. frigidimarina NCIMB400 and S. oneidensis MR-1 are soluble and monomeric enzymes located in the periplasm of these bacteria. These proteins display two redox active domains, one containing four c-type hemes and another
Publikováno v:
Biochemical Society Transactions
Thackray, S J, Mowat, C G & Chapman, S K 2008, ' Exploring the mechanism of tryptophan 2,3-dioxygenase ', Biochemical Society Transactions, vol. 36, pp. 1120-1123 . https://doi.org/10.1042/BST0361120
Thackray, S J, Mowat, C G & Chapman, S K 2008, ' Exploring the mechanism of tryptophan 2,3-dioxygenase ', Biochemical Society Transactions, vol. 36, pp. 1120-1123 . https://doi.org/10.1042/BST0361120
The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathwa
Autor:
Stephen K Chapman, J. L. Ross Anderson, Graeme A Reid, Bor Ran Li, Caroline S Miles, Christopher G. Mowat
Publikováno v:
Biochemical Society Transactions. 36:992-995
Rhodobacter sphaeroides produces a novel cytochrome, designated as SHP (sphaeroides haem protein), that is unusual in having asparagine as a redox-labile haem ligand. The gene encoding SHP is contained within an operon that also encodes a DHC (dihaem
Autor:
Anne K. Jones, Christopher G. Mowat, Katherine L Pankhurst, Malcolm D. Walkinshaw, Stephen K Chapman, Caroline S Miles, Fraser A. Armstrong, Emma L Rothery, Graeme A Reid, Janette M. Hudson
Publikováno v:
Journal of Biological Chemistry. 281:20589-20597
The mechanism for fumarate reduction by the soluble fumarate reductase from Shewanella frigidimarina involves hydride transfer from FAD and proton transfer from the active-site acid, Arg-402. It has been proposed that Arg-402 forms part of a proton t
Autor:
Stephen K Chapman, Ker R. Marshall, Mattias C. U. Gustafsson, Claes von Wachenfeldt, Olivier Roitel, Antonio M Pessegueiro, Myles R Cheesman, Michael A. Noble, Armand J. Fulco, Andrew W. Munro
Publikováno v:
Biochemistry. 43:5474-5487
The cyp102A2 and cyp102A3 genes encoding the two Bacillus subtilis homologues (CYP102A2 and CYP102A3) of flavocytochrome P450 BM3 (CYP102A1) from Bacillus megaterium have been cloned, expressed in Escherichia coli, purified, and characterized spectro
Autor:
Simon Daff, Caroline S Miles, Christopher G. Mowat, Jonathan P. Clark, Graeme A Reid, Stephen K Chapman, Malcolm D. Walkinshaw, Tobias W B Ost
Publikováno v:
Journal of the American Chemical Society. 125:15010-15020
In flavocytochrome P450 BM3, there is a conserved phenylalanine residue at position 393 (Phe393), close to Cys400, the thiolate ligand to the heme. Substitution of Phe393 by Ala, His, Tyr, and Trp has allowed us to modulate the reduction potential of
Publikováno v:
The Biochemist. 25:20-23
More than one-third of all enzymes catalyse the oxidation or reduction of a substrate and are therefore classed as oxidoreductases or redox enzymes. The, often complex, redox chemistry involved here is made possible by surprisingly few redox-active c