Mechanism and dynamics of fatty acid photodecarboxylase

Sorigué, Damien; Hadjidemetriou, Kyprianos; Blangy, Stéphanie; Gotthard, Guillaume; Bonvalet, Adeline; Coquelle, Nicolas; Samire, Poutoum; Aleksandrov, Alexey; Antonucci, L.; Benachir, A.; Boutet, Sébastien; Byrdin, Martin; Cammarata, Marco; Carbajo, Sergio; Cuiné, Stéphan; Doak, R. Bruce; Foucar, L.; Gorel, A.; Grünbein, Marie Luise; Hartmann, Elisabeth; Hienerwadel, Rainer; Hilpert, M.; Kloos, Marco; Lane, Thomas J; Légeret, Bertrand; Legrand, Pierre; Li‐Beisson, Yonghua; Moulin, Solène; Nurizzo, Didier; Peltier, Gilles; Schirò, Giorgio; Shoeman, Robert L.; Śliwa, M.; Solinas, Xavier; Zhuang, B. A.; Barends, Thomas R. M.; Colletier, Jacques‐Philippe; Joffre, Manuel; Royant, Antoine; Berthomieu, Catherine; Weik, Martin H.; Domratcheva, Tatiana; Brettel, Klaus; Vos, Marten H.; Schlichting, Ilme; Arnoux, Pascal; Müller, Pavel; Beisson, Frédéric

doi:10.1126/science.abd5687

Cited by 108 publications

(175 citation statements)

References 124 publications

(137 reference statements)

Supporting

Mentioning

157

Contrasting

Unclassified

Order By: Relevance

“…In blue light receptor proteins, such as cryptochromes and blue light using flavin (BLUF) domain proteins, the photoreduction of oxidized flavin (FMN ox or FAD ox ) to the anionic radical form (FMN •− or FAD •− ) represents the first essential step in their response to light ( 19 , 20 ). In fatty acid photodecarboxylase, the photoinduced ET between FAD ox and the fatty acid substrate leads to FAD •− as an intermediate ( 21 ). The catalytic activity of the flavoprotein monooxygenase PqsL can be triggered by blue light illumination, which was proposed to occur via photoinduced formation of the NAD(P)H •+ /FAD •− radical pair ( 22 ).…”

mentioning

confidence: 99%

Ultrafast photooxidation of protein-bound anionic flavin radicals

Zhuang

Ramodiharilafy

Liebl

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

The photophysical properties of anionic semireduced flavin radicals are largely unknown despite their importance in numerous biochemical reactions. Here, we studied the photoproducts of these intrinsically unstable species in five different flavoprotein oxidases where they can be stabilized, including the well-characterized glucose oxidase. Using ultrafast absorption and fluorescence spectroscopy, we unexpectedly found that photoexcitation systematically results in the oxidation of protein-bound anionic flavin radicals on a time scale of less than ∼100 fs. The thus generated photoproducts decay back in the remarkably narrow 10- to 20-ps time range. Based on molecular dynamics and quantum mechanics computations, positively charged active-site histidine and arginine residues are proposed to be the electron acceptor candidates. Altogether, we established that, in addition to the commonly known and extensively studied photoreduction of oxidized flavins in flavoproteins, the reverse process (i.e., the photooxidation of anionic flavin radicals) can also occur. We propose that this process may constitute an excited-state deactivation pathway for protein-bound anionic flavin radicals in general. This hitherto undocumented photochemical reaction in flavoproteins further extends the family of flavin photocycles.

show abstract

mentioning

confidence: 99%

Ultrafast photooxidation of protein-bound anionic flavin radicals

Zhuang

Ramodiharilafy

Liebl

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

show abstract

“…The catalytic cycle is closed by an electron transfer from FAD •− to the amino acid radical (Scheme 1 ). [ 1b , 6 ]…”

mentioning

confidence: 99%

“…In accordance with the Cv FAP inactivation mechanism proposed by Scrutton and co‐workers, [8] our results indicate that photoexcitation of Cv FAP in the absence of a convertible substrate (carboxylic acid) represents the main cause for Cv FAP photoinactivation. In this situation, the photoexcited flavin oxidises active‐site borne amino acids, which in light of the recent mechanistic studies by Beisson and co‐workers, [1b] may be the catalytically active cysteine or arginine (Scheme 2 ).…”

mentioning

confidence: 99%

Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid

Paul

Hollmann

2021

ChemBioChem

View full text Add to dashboard Cite

The fatty acid photodecarboxylase from Chlorella variabilis NC64 A (CvFAP) catalyses the light-dependent decarboxylation of fatty acids. Photoinactivation of CvFAP still represents one of the major limitations of this interesting enzyme en route to practical application. In this study we demonstrate that the photostability of CvFAP can easily be improved by the administration of medium-chain length carboxylic acids such as caprylic acid indicating that the best way of maintaining CvFAP stability is 'to keep the enzyme busy'.

show abstract

“…Indeed, the newly discovered Fatty Acid Photodecarboxylase (FAP) also harbours a flavin cofactor involved in electron and proton transfer reactions with the substrate. Klaus' expertise allowed the initiation of the elucidation of the intricate kinetic steps in this photoenzymatic reaction [116,117]. Thus, again the happy combination of a spectroscopist's skill and a physico-chemists insight allowed unravelling one more aspect of light-induced electron transfer.…”

Section: Forty Years At the Crossroads Of Means And Ends (By Mb)mentioning

confidence: 99%

Pushing the limits of flash photolysis to unravel the secrets of biological electron and proton transfer

Mathis

Sage

Byrdin

2022

Photochem Photobiol Sci

View full text Add to dashboard Cite

Time-resolved absorption spectroscopy is a powerful tool to unravel biological functions and has been a key technology for elucidating the working of electron transfer chains in photosynthesis or photorepair of UV-damaged DNA. Both of these areas have seen important contributions from laboratories all over the world, not the least of them stemming from the ingenious technical advances described by Klaus Brettel, first at the Technical University of Berlin (Germany), and later at the Atomic Energy Agency in Saclay (France). Now, after more than forty years of tireless scientific activity, Klaus is approaching retirement and this collection gathers together tributes in the form of scientific contributions from colleagues along the way, covering a spectrum of topics as diverse as photosynthesis, light-induced DNA repair, electron and proton transfer in light signalling, flavin based photo-enzymology, fluorescent marker photophysics, synthetic models and modelisation, delicate sample transient absorption spectroscopy. In an era where science is increasingly changing context from "fundamental" to "applied", Klaus' curiosity and tenacity worked hand in hand in a most effective manner to further both technical possibilities and basic understanding.

show abstract

Mechanism and dynamics of fatty acid photodecarboxylase

Cited by 108 publications

References 124 publications

Ultrafast photooxidation of protein-bound anionic flavin radicals

Ultrafast photooxidation of protein-bound anionic flavin radicals

Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid

Pushing the limits of flash photolysis to unravel the secrets of biological electron and proton transfer

Contact Info

Product

Resources

About