Mechanism and dynamics of fatty acid photodecarboxylase

Sorigué, D; Hadjidemetriou, K; Blangy, S; Gotthard, G; Bonvalet, A; Coquelle, N; Samire, P; Aleksandrov, A; Antonucci, L; Benachir, A; Boutet, S; Byrdin, M; Cammarata, M; Carbajo, S; Cuiné, S; Doak, R B; Foucar, L; Gorel, A; Grünbein, M; Hartmann, E; Hienerwadel, R; Hilpert, M; Kloos, M; Lane, T J; Légeret, B; Legrand, P; Li-Beisson, Y; Moulin, S L Y; Nurizzo, D; Peltier, G; Schirò, G; Shoeman, R L; Sliwa, M; Solinas, X; Zhuang, B; Barends, T R M; Colletier, J-P; Joffre, M; Royant, A; Berthomieu, C; Weik, M; Domratcheva, T; Brettel, K; Vos, M H; Schlichting, I; Arnoux, P; Müller, P; Beisson, F

doi:10.1126/science.abd5687

Datensatz

DATENSATZ AKTIONENEXPORT

Zur Ablage hinzufügen

Bitte beachten Sie, dass eine neuere Version dieses Datensatzes verfügbar ist:
https://pure.mpg.de/pubman/item/item_3310685_4

DetailsÜbersicht

Freigegeben

Zeitschriftenartikel

Mechanism and dynamics of fatty acid photodecarboxylase

MPG-Autoren

/persons/resource/persons117878

Doak, R B
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92933

Foucar, L
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons192083

Gorel, A
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons123592

Grünbein, M
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117815

Hartmann, E
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183393

Hilpert, M
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons203860

Kloos, M
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95345

Shoeman, R L
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92083

Barends, T R M
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92695

Domratcheva, T
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95189

Schlichting, I
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://science.sciencemag.org/content/372/6538/eabd5687/tab-pdf
(beliebiger Volltext)

https://doi.org/10.1126/science.abd5687
(beliebiger Volltext)

Volltexte (beschränkter Zugriff)

Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.

Volltexte (frei zugänglich)

Es sind keine frei zugänglichen Volltexte in PuRe verfügbar

Ergänzendes Material (frei zugänglich)

Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar

Zitation

Sorigué, D., Hadjidemetriou, K., Blangy, S., Gotthard, G., Bonvalet, A., Coquelle, N., et al. (2021). Mechanism and dynamics of fatty acid photodecarboxylase. Science, 372(6538): eabd5687, pp. 1-13. doi:10.1126/science.abd5687.

Zitierlink: https://hdl.handle.net/21.11116/0000-0008-4C5C-D

Zusammenfassung

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.