Zobrazeno 1 - 10
of 144
pro vyhledávání: '"Stephen E. J. Rigby"'
Autor:
Mary Ortmayer, Florence J. Hardy, Matthew G. Quesne, Karl Fisher, Colin Levy, Derren J. Heyes, C. Richard A. Catlow, Sam P. de Visser, Stephen E. J. Rigby, Sam Hay, Anthony P. Green
Publikováno v:
JACS Au, Vol 1, Iss 7, Pp 913-918 (2021)
Externí odkaz:
https://doaj.org/article/7b1ea1dfa43042aa99a9e11ae0aa8261
Autor:
Stephen A. Marshall, Karl A. P. Payne, Karl Fisher, Mark D. White, Aisling Ní Cheallaigh, Arune Balaikaite, Stephen E. J. Rigby, David Leys
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
The UbiD-UbiX decarboxylase system is required for the biosynthesis of quinone cofactors. Here, the authors combine structural and biochemical analyses to elucidate the UbiX reaction mechanism, showing that it resembles the mode of action of class I
Externí odkaz:
https://doaj.org/article/7d6536e8acd943bea50c5023037c7730
Autor:
George J. Baker, Hazel M. Girvan, Sarah Matthews, Kirsty J. McLean, Marina Golovanova, Timothy N. Waltham, Stephen E. J. Rigby, David R. Nelson, Richard T. Blankley, Andrew W. Munro
Publikováno v:
ACS Omega, Vol 2, Iss 8, Pp 4705-4724 (2017)
Externí odkaz:
https://doaj.org/article/9d2e711fc5a24b71bb75ed933c0f3c61
Publikováno v:
Microorganisms, Vol 8, Iss 9, p 1344 (2020)
Reductive dehalogenases are responsible for the reductive cleavage of carbon-halogen bonds during organohalide respiration. A variety of mechanisms have been proposed for these cobalamin and [4Fe-4S] containing enzymes, including organocobalt, radica
Externí odkaz:
https://doaj.org/article/e93318ce82b545cd9a859c138833f72b
Autor:
Diego M. Cannas, Sam Hay, Stephen E. J. Rigby, Karl Fisher, David Leys, Reynard Spiess, Stephen A. Marshall, Matthew J. Cliff, Igor Larrosa, Karl A. P. Payne
Publikováno v:
ACS Catalysis
Payne, K A P, Marshall, S A, Fisher, K, Rigby, S E J, Cliff, M J, Spiess, R, Cannas, D M, Larrosa, I, Hay, S & Leys, D 2021, ' Structure and Mechanism of Pseudomonas aeruginosa PA0254/HudA, a prFMN-Dependent Pyrrole-2-carboxylic Acid Decarboxylase Linked to Virulence ', ACS Catalysis, vol. 11, no. 5, pp. 2865-2878 . https://doi.org/10.1021/acscatal.0c05042
Payne, K A P, Marshall, S A, Fisher, K, Rigby, S E J, Cliff, M J, Spiess, R, Cannas, D M, Larrosa, I, Hay, S & Leys, D 2021, ' Structure and Mechanism of Pseudomonas aeruginosa PA0254/HudA, a prFMN-Dependent Pyrrole-2-carboxylic Acid Decarboxylase Linked to Virulence ', ACS Catalysis, vol. 11, no. 5, pp. 2865-2878 . https://doi.org/10.1021/acscatal.0c05042
The UbiD family of reversible (de)carboxylases depends on the recently discovered prenylated-FMN (prFMN) cofactor for activity. The model enzyme ferulic acid decarboxylase (Fdc1) decarboxylates unsaturated aliphatic acids via a reversible 1,3-cycload
Publikováno v:
Methods in enzymology. 668
Reductive dehalogenases provide a possible route to the biotechnological remediation of widespread anthropogenic environmental organohalide contamination. These bacterial enzymes employ cobalamin and an internal electron transfer chain of two [4Fe-4S
Autor:
Matthew G. Quesne, Florence J. Hardy, Stephen E. J. Rigby, Sam Hay, C. Richard A. Catlow, Sam P. de Visser, Karl Fisher, Colin Levy, Anthony P. Green, Derren J. Heyes, Mary Ortmayer
Publikováno v:
JACS Au, Vol 1, Iss 7, Pp 913-918 (2021)
JACS Au
JACS Au
Nature employs high-energy metal-oxo intermediates embedded within enzyme active sites to perform challenging oxidative transformations with remarkable selectivity. Understanding how different local metal-oxo coordination environments control interme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ea5cd79aab625181d24c7a852691fc9
https://orca.cardiff.ac.uk/id/eprint/143856/1/jacsau.1c00145.pdf
https://orca.cardiff.ac.uk/id/eprint/143856/1/jacsau.1c00145.pdf
Publikováno v:
Protein Expression and Purification
Halliwell, T, Fisher, K, Payne, K, Rigby, S E J & Leys, D 2021, ' Heterologous expression of cobalamin dependent class-III enzymes ', Protein Expression and Purification, vol. 177, 105743, pp. 105743 . https://doi.org/10.1016/j.pep.2020.105743
Halliwell, T, Fisher, K, Payne, K, Rigby, S E J & Leys, D 2021, ' Heterologous expression of cobalamin dependent class-III enzymes ', Protein Expression and Purification, vol. 177, 105743, pp. 105743 . https://doi.org/10.1016/j.pep.2020.105743
The family of cobalamin class-III dependent enzymes is composed of the reductive dehalogenases (RDases) and related epoxyqueuosine reductases. RDases are crucial for the energy conserving process of organohalide respiration. These enzymes have the ab
Autor:
Karl A P, Payne, Stephen A, Marshall, Karl, Fisher, Stephen E J, Rigby, Matthew J, Cliff, Reynard, Spiess, Diego M, Cannas, Igor, Larrosa, Sam, Hay, David, Leys
Publikováno v:
ACS Catalysis
The UbiD family of reversible (de)carboxylases depends on the recently discovered prenylated-FMN (prFMN) cofactor for activity. The model enzyme ferulic acid decarboxylase (Fdc1) decarboxylates unsaturated aliphatic acids via a reversible 1,3-cycload
Publikováno v:
Microorganisms
Volume 8
Issue 9
Halliwell, T, Fisher, K, Payne, K A P, Rigby, S E J & Leys, D 2020, ' Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope ', Microorganisms, vol. 8, no. 9 . https://doi.org/10.3390/microorganisms8091344
Microorganisms, Vol 8, Iss 1344, p 1344 (2020)
Volume 8
Issue 9
Halliwell, T, Fisher, K, Payne, K A P, Rigby, S E J & Leys, D 2020, ' Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope ', Microorganisms, vol. 8, no. 9 . https://doi.org/10.3390/microorganisms8091344
Microorganisms, Vol 8, Iss 1344, p 1344 (2020)
Reductive dehalogenases are responsible for the reductive cleavage of carbon-halogen bonds during organohalide respiration. A variety of mechanisms have been proposed for these cobalamin and [4Fe-4S] containing enzymes, including organocobalt, radica