Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Caroline S Miles"'
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:
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:
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:
Christopher C. Moser, Tobias W B Ost, Simon Daff, Dominikus A. Lysek, Caroline S Miles, Stephen K Chapman, Kirsty J. McLean, P. Leslie Dutton, David Leys, Ker R. Marshall, Andrew W. Munro, Christopher C. Page
Publikováno v:
Trends in Biochemical Sciences. 27:250-257
Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion
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:
Mary K. Doherty, R Moysey, Stephen K Chapman, Caroline S Miles, Emma L Rothery, Katherine L Pankhurst, Graeme A Reid
Publikováno v:
Journal of Inorganic Biochemistry. 86:361-370
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1543:383-407
The cytochromes P-450 are an immensely important superfamily of heme-containing enzymes. They catalyze the monooxygenation of an enormous range of substrates. In bacteria, cytochromes P-450 are known to catalyze the hydroxylation of environmentally s
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:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1459(2-3):310-315
In the absence of oxygen many bacteria are able to utilise fumarate as a terminal oxidant for respiration. In most known organisms the fumarate reductases are membrane-bound iron-sulfur flavoproteins but Shewanella species produce a soluble, periplas