{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T11:17:30Z","timestamp":1788434250850,"version":"build-2803163510"},"reference-count":62,"publisher":"American Chemical Society (ACS)","issue":"17","license":[{"start":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T00:00:00Z","timestamp":1787443200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T00:00:00Z","timestamp":1787443200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T00:00:00Z","timestamp":1787443200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Cryptochromes act as photoreceptors in diverse organisms and bind flavin adenine dinucleotide (FAD) as a chromophore. The plant-like cryptochrome CryP from the diatom Phaeodactylum tricornutum regulates in vivo the expression of light-harvesting proteins in response to blue light. CryP carries, in addition, 5,10-methenyltetrahydrofolate (MTHF) for light capturing. In contrast to most other cryptochromes, FAD in CryP is present as a stable flavin neutral radical in the dark, which undergoes a photoreduction to form the fully reduced state in the light. Here, we demonstrate by applying nanosecond-time-resolved UV\u2013vis spectroscopy that the flavin neutral radical is photoreduced within 100 ns to the fully reduced state and subsequently recovers very fast with a time constant of 1.4 ms in the absence of reducing agents or in the presence of 1 mM dithiothreitol. Despite its short lifetime, the transient light state is sufficient to induce homo-oligomerization of CryP as shown by light-dependent size exclusion chromatography. A long-lived fully reduced flavin is only formed in the presence of external reducing agents by a second pathway that is lost after a single full conversion, likely by degradation. Then, the recovery to the neutral radical state takes hours with a time constant of 40 min. Moreover, we validate the existence of energy transfer between the two chromophores depending on the flavin redox state using fluorescence spectroscopy. We propose a detailed mechanism for the photocycle of CryP, highlighting the contribution of two separate reduction pathways.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00479","type":"journal-article","created":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T12:25:01Z","timestamp":1787919901000},"page":"2756-2768","source":"Crossref","is-referenced-by-count":0,"title":["The Photocycle\nof the Red Light-Sensitive Plant-like\nCryptochrome CryP from\n                    <i>Phaeodactylum tricornutum<\/i>"],"prefix":"10.1021","volume":"65","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-1671-0896","authenticated-orcid":true,"given":"Marius F.","family":"Nagel","sequence":"first","affiliation":[{"name":"Bielefeld University , , Universita\u0308tsstra\u00dfe 25 , ,","place":["Bielefeld, Germany, 33615"]},{"name":"Bielefeld University , , Universita\u0308tsstra\u00dfe 25 , ,","place":["Bielefeld, Germany, 33615"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maximilian","family":"Steiner","sequence":"additional","affiliation":[{"name":"Bielefeld University , , Universita\u0308tsstra\u00dfe 25 , ,","place":["Bielefeld, Germany, 33615"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Niklas C. J.","family":"Wenner","sequence":"additional","affiliation":[{"name":"Bielefeld University , , Universita\u0308tsstra\u00dfe 25 , ,","place":["Bielefeld, Germany, 33615"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6640-7610","authenticated-orcid":true,"given":"Claudia","family":"Bu\u0308chel","sequence":"additional","affiliation":[{"name":"Goethe University Frankfurt , , Max-von-Laue-Str. 9 , ,","place":["Frankfurt, Germany, 60438"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8080-9579","authenticated-orcid":true,"given":"Tilman","family":"Kottke","sequence":"additional","affiliation":[{"name":"Bielefeld University , , Universita\u0308tsstra\u00dfe 25 , ,","place":["Bielefeld, Germany, 33615"]},{"name":"Bielefeld University , , Universita\u0308tsstra\u00dfe 25 , ,","place":["Bielefeld, Germany, 33615"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,23]]},"reference":[{"key":"2026090306405182700_cit1","doi-asserted-by":"publisher","first-page":"2203","DOI":"10.1021\/cr0204348","article-title":"Structure\nand function of DNA photolyase and cryptochrome blue-light photoreceptors","volume":"103","author":"Sancar","year":"2003","journal-title":"Chem. 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Exp.\nBot."},{"key":"2026090306405182700_cit28","doi-asserted-by":"publisher","first-page":"1041","DOI":"10.1021\/bi401599z","article-title":"Response of\nthe sensory animal-like cryptochrome aCRY to blue and red light as\nrevealed by infrared difference spectroscopy","volume":"53","author":"Spexard","year":"2014","journal-title":"Biochemistry"},{"key":"2026090306405182700_cit29","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1016\/j.jmb.2011.08.031","article-title":"Light-induced conformational changes\nin full-length Arabidopsis thaliana cryptochrome","volume":"413","author":"Kondoh","year":"2011","journal-title":"J. Mol. 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B"},{"key":"2026090306405182700_cit45","doi-asserted-by":"publisher","first-page":"12142","DOI":"10.1073\/pnas.0404851101","article-title":"Structure\nof the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana","volume":"101","author":"Brautigam","year":"2004","journal-title":"Proc.\nNatl. Acad. Sci. U.S.A."},{"key":"2026090306405182700_cit46","doi-asserted-by":"publisher","first-page":"12647","DOI":"10.1002\/anie.201104321","article-title":"Unexpected Electron Transfer in Cryptochrome\nIdentified by Time-Resolved EPR Spectroscopy","volume":"50","author":"Biskup","year":"2011","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026090306405182700_cit47","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1016\/j.bpj.2016.06.009","article-title":"Extended electron-transfer in animal\ncryptochromes mediated by a tetrad of aromatic amino acids","volume":"111","author":"Nohr","year":"2016","journal-title":"Biophys. 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Soc."},{"key":"2026090306405182700_cit52","doi-asserted-by":"publisher","first-page":"3175","DOI":"10.1111\/febs.13299","article-title":"Spectroscopic\ncharacterization of radicals and radical pairs in fruit fly cryptochrome\u2500protonated\nand nonprotonated flavin radical-states","volume":"282","author":"Paulus","year":"2015","journal-title":"FEBS\nJ."},{"key":"2026090306405182700_cit53","doi-asserted-by":"publisher","first-page":"1329","DOI":"10.1021\/jp044652b","article-title":"Femtosecond\ndynamics of flavin cofactor in DNA photolyase: Radical reduction,\nlocal solvation, and charge recombination","volume":"109","author":"Wang","year":"2005","journal-title":"J.\nPhys. Chem. B"},{"key":"2026090306405182700_cit54","doi-asserted-by":"publisher","first-page":"28767","DOI":"10.1039\/C8CP04671A","article-title":"The sacrificial inactivation of the\nblue-light photosensor cryptochrome from Drosophila melanogaster","volume":"20","author":"Kutta","year":"2018","journal-title":"Phys. Chem. 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