{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T05:18:50Z","timestamp":1787894330997,"version":"build-2784847793"},"reference-count":37,"publisher":"Wiley","issue":"16","license":[{"start":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T00:00:00Z","timestamp":1787702400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T00:00:00Z","timestamp":1787702400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemBioChem"],"published-print":{"date-parts":[[2026,8,27]]},"abstract":"<jats:p>\n                    Plant cryptochromes are blue light\u2010responsive photoreceptor proteins that regulate various photoresponses throughout plant growth and development. Compared with their homologous CPD I\/III photolyases, plant cryptochromes have lost DNA repair activity but evolved signal transduction functions. The structurally conserved ligand\u2010binding pocket, which corresponds to the photolyase active site, exhibits distinctive features in plant cryptochromes, with key binding residues being altered relative to photolyases. Notably, the distribution of charged amino acids around this pocket differs markedly between the two protein families. In this study, we identified two conserved positively charged residues (Arg237 and Arg357) flanking this pocket in\n                    <jats:italic>Chlamydomonas reinhardtii<\/jats:italic>\n                    cryptochrome (pCRY) and its\n                    <jats:italic>Arabidopsis<\/jats:italic>\n                    homologs. Biochemical and physiological analyses demonstrated that these residues effectively modulate photoreduction kinetics and oxidative stability of the flavin adenine dinucleotide (FAD) cofactor, participate in ATP binding, and ultimately influence flowering time in transgenic\n                    <jats:italic>Arabidopsis<\/jats:italic>\n                    plants. Our findings reveal that these conserved positively charged sites play critical roles in regulating the photosensitivity and functional stability of plant cryptochromes.\n                  <\/jats:p>","DOI":"10.1002\/cbic.202500946","type":"journal-article","created":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T12:55:25Z","timestamp":1787748925000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Functional Characterization of Conserved Positively Charged Residues Surrounding the Ligand\u2010Binding Pocket in Plant Cryptochromes"],"prefix":"10.1002","volume":"27","author":[{"given":"Mengqi","family":"Wan","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, School of Basic Medicine Wannan Medical College  Wuhu Anhui China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hao","family":"Liu","sequence":"additional","affiliation":[{"name":"Department of 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