Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Wouter Laan"'
Autor:
Emma K. Gibson, Peter P. Wells, Paul C. J. Kamer, Peter J. Deuss, Lorenz Obrecht, Wouter Laan, Amanda G. Jarvis
Publikováno v:
Angewandte Chemie-International Edition, 56(44), 13596-13600. WILEY-V C H VERLAG GMBH
Jarvis, A G, Obrecht, L, Deuss, P J, Laan, W, Gibson, E K, Wells, P P & Kamer, P C J 2017, ' Enzyme Activity by Design: An Artificial Rhodium Hydroformylase for Linear Aldehydes ', Angewandte Chemie International Edition, vol. 56, no. 44, pp. 13596-13600 . https://doi.org/10.1002/anie.201705753
Angewandte Chemie (International Ed. in English)
Angewandte Chemie International Edition
Jarvis, A G, Obrecht, L, Deuss, P J, Laan, W, Gibson, E K, Wells, P P & Kamer, P C J 2017, ' Enzyme Activity by Design: An Artificial Rhodium Hydroformylase for Linear Aldehydes ', Angewandte Chemie International Edition, vol. 56, no. 44, pp. 13596-13600 . https://doi.org/10.1002/anie.201705753
Angewandte Chemie (International Ed. in English)
Angewandte Chemie International Edition
Funding: Marie Curie Individual Fellowship project ArtOxiZymes to AGJ (contract no. H2020-MSCA-IF-2014-657755), EPSRC Critical mass grant ‘Clean catalysis for sustainable development’ (EP/J018139/1) and Sasol (CASE studentship to P.J.D.), EPSRC (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecabedde887e47f56dfaa5202712f95b
https://eprints.soton.ac.uk/413631/
https://eprints.soton.ac.uk/413631/
Publikováno v:
ChemCatChem. 5:1184-1191
Publikováno v:
Catal. Sci. Technol.. 3:541-551
The biphasic hydroformylation of linear alkenes using the Rh–TPPTS catalyst system is one of the cornerstones of aqueous biphasic catalysis, but due to mass-transfer limitations its application is restricted to short alkenes. This perspective provi
Publikováno v:
Phosphorus(III) Ligands in Homogeneous Catalysis: Design and Synthesis. :481-496
Publikováno v:
Dalton Transactions, 39(36), 8477-8483. Royal Society of Chemistry
The preparation of hybrid transition metalloproteins by thiol-selective incorporation of organometallic rhodium- and ruthenium complexes is described. Phosphine ligands and two rhodium-diphosphine complexes bearing a carboxylic acid group were couple
Autor:
Robert Kaptein, Jeffrey S. Grinstead, Klaas J. Hellingwerf, Magdalena Gauden, Wouter Laan, Rolf Boelens, K.C. Toh, John T. M. Kennis, Ivo H. M. van Stokkum, Rienk van Grondelle, Marcela Avila-Perez
Publikováno v:
Biochemistry, 46, 7405-7415. American Chemical Society
Gauden, M L, Grinstead, J S, Laan, W, van Stokkum, H M, Avila-Perez, M, Toh, K C, Boelens, R, Kaptein, R, van Grondelle, R, Hellingwerf, K J & Kennis, J T M 2007, ' On the role of aromatic side chains in the photoactivation of BLUF domains ', Biochemistry, vol. 46, no. 25, pp. 7405-7415 . https://doi.org/10.1021/bi7006433
Biochemistry, 46(25), 7405-7415. American Chemical Society
Gauden, M L, Grinstead, J S, Laan, W, van Stokkum, H M, Avila-Perez, M, Toh, K C, Boelens, R, Kaptein, R, van Grondelle, R, Hellingwerf, K J & Kennis, J T M 2007, ' On the role of aromatic side chains in the photoactivation of BLUF domains ', Biochemistry, vol. 46, no. 25, pp. 7405-7415 . https://doi.org/10.1021/bi7006433
Biochemistry, 46(25), 7405-7415. American Chemical Society
BLUF (blue-light sensing using FAD) domain proteins are a novel group of blue-light sensing receptors found in many microorganisms. The role of the aromatic side chains Y21 and W104, which are in close vicinity to the FAD cofactor in the AppA BLUF do
Autor:
M.A. van der Horst, Klaas J. Hellingwerf, Wouter Laan, Andy Wende, S. Yeremenko, Peter Palm, Dieter Oesterhelt
Publikováno v:
Photochemical & Photobiological Sciences, 9, 688-693. Royal Society of Chemistry
To properly respond to changes in fluency conditions, Nature has developed a variety of photosensors that modulate gene expression, enzyme activity and/or motility. Dedicated types have evolved, which can be classified in six families: rhodopsins, ph
Publikováno v:
Photochemical & Photobiological Sciences, 3(11-12), 1011-1016. Royal Society of Chemistry
Upon heterologous expression of the BLUF (for: Blue-Light sensing Using Flavin) domain from AppA, a transcriptional anti-repressor from Rhodobacter sphaeroides, in Escherichia coli, photoactive holo-protein is formed through non-covalent binding of a
Publikováno v:
Photochemistry and Photobiology, 78(3), 290-297. Wiley-Blackwell
Laan, W, Horst, M A, van Stokkum, I H M & Hellingwerf, K J 2003, ' Initial characterization of the primary photochemistry of AppA, a blue-light-using flavin adenine dinucleotide-domain containing transcriptional antirepressor protein from Rhodobacter sphaeroides: A key role for reversible intramolecular proton transfer from the flavin adenine dinucleotide chromophore to a conserved tyrosine? ', Photochemistry and Photobiology, vol. 78, no. 3, pp. 290-297 . https://doi.org/10.1562/0031-8655(2003)078<0290:ICOTPP>2.0.CO;2
Laan, W, Horst, M A, van Stokkum, I H M & Hellingwerf, K J 2003, ' Initial characterization of the primary photochemistry of AppA, a blue-light-using flavin adenine dinucleotide-domain containing transcriptional antirepressor protein from Rhodobacter sphaeroides: A key role for reversible intramolecular proton transfer from the flavin adenine dinucleotide chromophore to a conserved tyrosine? ', Photochemistry and Photobiology, vol. 78, no. 3, pp. 290-297 . https://doi.org/10.1562/0031-8655(2003)078<0290:ICOTPP>2.0.CO;2
The flavin adenine dinucleotide (FAD)-containing photoreceptor protein AppA (in which the FAD is bound to a novel so-called BLUF domain) from the purple nonsulfur bacterium Rhodobacter sphaeroides was previously shown to be photoactive by the formati
Publikováno v:
Angewandte Chemie. 122:5443-5445