Layered bismuthene forming the interfacial pathway for rapid charge transfer in CuNb13O33/g-C3N5 photocatalyst for enhancing ciprofloxacin degradation

Autor: Siddiq, Hind Ahmed, Alhifthi, Amani, Ghubayra, Reem, Madkour, Metwally

Publikováno v: In Journal of Photochemistry & Photobiology, A: Chemistry 1 February 2025 459

Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from Rhizobium leguminosarum.

Autor: Li, Jinling, Sharma, Mahima, Meek, Richard, Alhifthi, Amani, Armstrong, Zachary, Soler, Niccolay Madiedo, Lee, Mihwa, Goddard-Borger, Ethan D., Blaza, James N., Davies, Gideon J., Williams, Spencer J.

Publikováno v: Chemical Science; 11/7/2023, Vol. 14 Issue 41, p11429-11440, 12p

Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase fromRhizobium leguminosarum

Autor: Jinling Li, Mahima Sharma, Richard Meek, Amani Alhifthi, Zachary Armstrong, Niccolay Madiedo Soler, Ethan D. Goddard-Borger, James N. Blaza, Gideon J. Davies, Spencer J. Williams

Sulfolactate (SL) is a short-chain organosulfonate that is an important reservoir of sulfur in the biosphere. SL is produced by oxidation of sulfolactaldehyde (SLA), which in turns derives from sulfoglycolysis of the sulfosugar sulfoquinovose, or thr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c43d6837048411697bd909da64fa1e51
https://doi.org/10.1101/2023.03.13.532361

Correction: Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from Rhizobium leguminosarum .

Autor: Li J; School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne Parkville Victoria 3010 Australia sjwill@unimelb.edu.au., Sharma M; York Structural Biology Laboratory, Department of Chemistry, University of York York YO10 5DD UK gideon.davies@york.ac.uk., Meek R; York Structural Biology Laboratory, Department of Chemistry, University of York York YO10 5DD UK gideon.davies@york.ac.uk., Alhifthi A; School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne Parkville Victoria 3010 Australia sjwill@unimelb.edu.au.; Chemistry Department, Faculty of Science (Female Section), Jazan University Jazan 82621 Saudi Arabia., Armstrong Z; School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne Parkville Victoria 3010 Australia sjwill@unimelb.edu.au., Soler NM; ACRF Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research Parkville Victoria 3010 Australia., Lee M; School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne Parkville Victoria 3010 Australia sjwill@unimelb.edu.au., Goddard-Borger ED; ACRF Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research Parkville Victoria 3010 Australia.; Department of Medical Biology, University of Melbourne Parkville Victoria 3010 Australia., Blaza JN; York Structural Biology Laboratory, Department of Chemistry, University of York York YO10 5DD UK gideon.davies@york.ac.uk., Davies GJ; York Structural Biology Laboratory, Department of Chemistry, University of York York YO10 5DD UK gideon.davies@york.ac.uk., Williams SJ; School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne Parkville Victoria 3010 Australia sjwill@unimelb.edu.au.

Publikováno v: Chemical science [Chem Sci] 2023 Dec 12; Vol. 15 (2), pp. 778-779. Date of Electronic Publication: 2023 Dec 12 (Print Publication: 2024).

Unimolecular, Bimolecular, and Intramolecular Hydrolysis Mechanisms of 4-Nitrophenyl β-d-Glucopyranoside

Autor: Amani Alhifthi, Spencer J. Williams

Publikováno v: The Journal of organic chemistry. 86(14)

1,2-trans-Glycosides hydrolyze through different mechanisms at different pH values, but systematic studies are lacking. Here, we report the pH-rate constant profile for the hydrolysis of 4-nitrophenyl β-D-glucoside. An inverse kinetic isotope effect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dab1b84120062b32148817b58b8d21f5
https://pubmed.ncbi.nlm.nih.gov/34190567