Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Stephen K Chapman"'
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:
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:
Zhi-wei Chen, F. S. Mathews, F E Welsh, J.D Barton, Graeme A Reid, Stephen K Chapman, L. M. Cunane
Publikováno v:
Biochemistry. 41:4264-4272
Flavocytochrome b2 catalyzes the oxidation of l-lactate to pyruvate and the transfer of electrons to cytochrome c. The enzyme consists of a flavin-binding domain, which includes the active site for lacate oxidation, and a b2-cytochrome domain, requir
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
Publikováno v:
Journal of Electroanalytical Chemistry. 500:598-603
The direct electrochemistry of the flavodehydrogenase domain of flavocytochrome b 2 engineered for l -mandelate dehydrogenase activity (FDH) has been investigated at an edge-plane pyrolytic graphite (EPG) electrode using poly- l -lysine as a promoter
Autor:
Stephen K Chapman, Scott P. Webster, Lisa McIver, Dominikus A. Lysek, Sharon M. Kelly, Robert Baxter, Dominic J. Campopiano, Claire Leadbeater, Michael A. Noble, Nicholas C. Price, Andrew W. Munro
Publikováno v:
Biochemical Journal. 352:257-266
The structure of the Escherichia coli flavodoxin NADP+ oxidoreductase (FLDR) places three arginines (R144, R174 and R184) in the proposed NADPH-binding site. Mutant enzymes produced by site-directed mutagenesis, in which each arginine was replaced by
Publikováno v:
Nature Structural Biology. 6:1108-1112
The 1.8 A resolution crystal structure of the tetraheme flavocytochrome c3, Fcc3, provides the first mechanistic insight into respiratory fumarate reductases or succinate dehydrogenases. The multi-redox center, three-domain protein shows a 40 A long
Autor:
Ikuko Sagami, Michael A. Noble, J. Guy Guillemette, Lesley J. Yellowlees, Laura Robledo, Shimizu Toru, Stephen K Chapman, Stuart L. Rivers, Simon N. Daff, Andrew W. Munro
Publikováno v:
Biochemistry. 38:16413-16418
Midpoint reduction potentials for the flavin cofactors in the reductase domain of rat neuronal nitric oxide synthase (nNOS) in calmodulin (CaM)-free and -bound forms have been determined by direct anaerobic titration. In the CaM-free form, the FMN po
Autor:
Stephen K Chapman, Rosli Md. Illias, Rhona Sinclair, Achim Neu, Graeme A Reid, Douglas J. Robertson
Publikováno v:
Biochemical Journal. 333:107-115
The l-mandelate dehydrogenase (L-MDH) from the yeast Rhodotorula graminis is a mitochondrial flavocytochrome b2 which catalyses the oxidation of mandelate to phenylglyoxylate coupled with the reduction of cytochrome c. We have used the N-terminal seq
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 3:246-252
Saccharomyces cerevisiae flavocytochrome b 2 couples the oxidation of L-lactate to the reduction of cytochrome c. The second-order rate constant for cytochrome c reduction by flavocytochrome b 2 depends on the rate of complex formation and is sensiti