Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Stephen K Chapman"'
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
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
Autor:
Stephen K Chapman, Stephen W.B. Fullerton, Simon Daff, Chris Whitfield, W. John Ingledew, James H. Naismith, David A. R. Sanders
Publikováno v:
Biochemistry. 42:2104-2109
UDP-galactopyranose mutase is a flavoprotein which catalyses the interconversion of UDP-galactopyranose and UDP-galactofuranose. The enzyme is of interest because it provides the activated biosynthetic precursor of galactofuranose, a key cell wall co
Autor:
Myles A. Cheesman, Christopher G. Mowat, Paul Taylor, Malcolm D. Walkinshaw, Stephen K Chapman, Andrew W. Munro, Arthur K. Cho, Antonio Pesseguiero, Armand J. Fulco, Tobias W B Ost
Publikováno v:
Biochemistry. 40:13430-13438
In the preceding paper in this issue [Ost, T. W. B., Miles, C. S., Munro, A. W., Murdoch, J., Reid, G. A., and Chapman, S. K. (2001) Biochemistry 40, 13421-13429], we have established that the primary role of the phylogenetically conserved phenylalan
Autor:
Mary K. Doherty, R Moysey, David Leys, Christopher G. Mowat, Stephen K Chapman, Caroline S Miles, Paul Taylor, Graeme A Reid, Malcolm D. Walkinshaw
Publikováno v:
Biochemistry. 40:12292-12298
There is now overwhelming evidence supporting a common mechanism for fumarate reduction in the respiratory fumarate reductases. The X-ray structures of substrate-bound forms of these enzymes indicate that the substrate is well positioned to accept a
Autor:
Graeme A Reid, Paul Taylor, Sara L. Pealing, Stephen K Chapman, Mary K. Doherty, R Moysey, Caroline S Miles, Malcolm D. Walkinshaw
Publikováno v:
Biochemistry. 39:10695-10701
The active sites of respiratory fumarate reductases are highly conserved, indicating a common mechanism of action involving hydride and proton transfer. Evidence from the X-ray structures of substrate-bound fumarate reductases, including that for the
Publikováno v:
Biochemistry. 39:4243-4249
Each monomer of the dimeric cytochrome cd(1) nitrite reductase from Paracoccus pantotrophus contains two hemes: one c-type center and one noncovalently bound d(1) center. Potentiometric analysis at 20 degrees C shows substantial cooperativity between
Autor:
Karen L. Turner, Stephen K Chapman, H A Heering, Mary K. Doherty, Graeme A Reid, Fraser A. Armstrong
Publikováno v:
Biochemistry. 38:3302-3309
The thermodynamic and catalytic properties of flavocytochrome c3 from Shewanella frigidimarina have been studied using a combination of protein film voltammetry and solution methods. As measured by solution kinetics, maximum catalytic efficiencies fo