Zobrazeno 41 - 50
of 194
pro vyhledávání: '"Stephen K Chapman"'
Autor:
Claus Jacob, Sonia Wilson, Timothy F. Booth, Alexander Y. Safronov, Stephen K Chapman, H. Allen O. Hill
Publikováno v:
Journal of Electroanalytical Chemistry. 430:119-125
A novel chiral redox-active ferrocene compound (FcV1) with amphiphilic properties has been synthesised and used successfully to form protein + lipid ‘clusters’ with ferritin and gold-labelled BSA. These structures could be observed by cryogenic t
Publikováno v:
Biochemical Journal. 316:507-513
The two domains of flavocytochrome b2 are connected by a typical hinge peptide. To probe the role of the hinge in modulating the efficiency of intraprotein electron transfer between these two domains, a number of mutant enzymes with truncated hinge r
Publikováno v:
Biochimie. 77:621-630
Flavocytochrome b2 catalyzes the two-electron oxidation of L-lactate. Reducing equivalents are transferred first to FMN then to heme b2 in the same subunit, finally to cytochrome c or a non-physiological acceptor. The enzyme's three-dimensional struc
Autor:
António V. Xavier, Katherine L Pankhurst, Emma L Rothery, Miguel Pessanha, Stephen K Chapman, Carlos A. Salgueiro, David L. Turner, Graeme A Reid
Publikováno v:
Inorganica Chimica Acta. 356:379-381
Flavocytochrome c3 is a periplasmic fumarate reductase with Mr 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme,
Autor:
Christopher G. Mowat, Emma Lloyd Raven, Igor Efimov, Jaswir Basran, Stephen K Chapman, Nishma Chauhan, Xiao Sun
Publikováno v:
Efimov, I, Basran, J, Sun, X, Chauhan, N, Chapman, S, Mowat, C & Raven, E 2012, ' The Mechanism of Substrate Inhibition in Human Indoleamine 2,3-Dioxygenase ', Journal of the American Chemical Society, vol. 134, no. 6, pp. 3034-3041 . https://doi.org/10.1021/ja208694g
Journal of the American Chemical Society
Journal of the American Chemical Society
Indoleamine 2,3-dioxygenase catalyzes the O2-dependent oxidation of l-tryptophan (l-Trp) toN-formylkynurenine (NFK) as part of the kynurenine pathway. Inhibition of enzyme activity at high l-Trp concentrations was first noted more than 30 years ago,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a7b8292ffd31721e4205eeca6fc7ffc
https://www.pure.ed.ac.uk/ws/files/8894316/ja208694g.pdf
https://www.pure.ed.ac.uk/ws/files/8894316/ja208694g.pdf
Autor:
Forbes D C Manson, R.E. Sharp, Patricia White, Graeme A Reid, Simon Daff, Stephen K Chapman, Florence Lederer
Publikováno v:
Biochemical Society Transactions. 22:713-718
Publikováno v:
Scopus-Elsevier
University of Manchester-PURE
University of Manchester-PURE
Flavocytochrome b2 from Saccharomyces cerevisiae acts physiologically as an L-lactate dehydrogenase. Although L-lactate is its primary substrate, the enzyme is also able to utilize a variety of other (S)-2-hydroxy acids. Structural studies and sequen
Publikováno v:
Biochemical Journal. 297:647-652
A detailed kinetic analysis of the oxidation of mono-substituted mandelates catalysed by L-(+)-mandelate dehydrogenase (L-MDH) from Rhodotorula graminis has been carried out to elucidate the role of the substrate in the catalytic mechanism. Values of
Autor:
Stephen K Chapman
Publikováno v:
Inorganica Chimica Acta. 331:xv-xvii