| Literature DB >> 33833098 |
D Sorigué1, K Hadjidemetriou2, S Blangy1, G Gotthard3, A Bonvalet4, N Coquelle5, P Samire1,6, A Aleksandrov4, L Antonucci4, A Benachir4, S Boutet7, M Byrdin2, M Cammarata8, S Carbajo7, S Cuiné1, R B Doak9, L Foucar9, A Gorel9, M Grünbein9, E Hartmann9, R Hienerwadel1, M Hilpert9, M Kloos10, T J Lane7, B Légeret1, P Legrand11, Y Li-Beisson1, S L Y Moulin1, D Nurizzo3, G Peltier1, G Schirò2, R L Shoeman9, M Sliwa12, X Solinas4, B Zhuang4,6, T R M Barends9, J-P Colletier2, M Joffre4, A Royant2,3, C Berthomieu13, M Weik14, T Domratcheva10,15, K Brettel6, M H Vos16, I Schlichting10, P Arnoux13, P Müller17, F Beisson13.
Abstract
Fatty acid photodecarboxylase (FAP) is a photoenzyme with potential green chemistry applications. By combining static, time-resolved, and cryotrapping spectroscopy and crystallography as well as computation, we characterized Chlorella variabilis FAP reaction intermediates on time scales from subpicoseconds to milliseconds. High-resolution crystal structures from synchrotron and free electron laser x-ray sources highlighted an unusual bent shape of the oxidized flavin chromophore. We demonstrate that decarboxylation occurs directly upon reduction of the excited flavin by the fatty acid substrate. Along with flavin reoxidation by the alkyl radical intermediate, a major fraction of the cleaved carbon dioxide unexpectedly transformed in 100 nanoseconds, most likely into bicarbonate. This reaction is orders of magnitude faster than in solution. Two strictly conserved residues, R451 and C432, are essential for substrate stabilization and functional charge transfer.Entities:
Year: 2021 PMID： 33833098 DOI： 10.1126/science.abd5687
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728