Nicotinamide Adenine Dinucleotides Arrest Photoreduction of Class II DNA Photolyases in FADH(center dot) State

DC FieldValueLanguage
dc.contributor.authorIgnatz, Elisabeth
dc.contributor.authorGeisselbrecht, Yann
dc.contributor.authorKiontke, Stephan
dc.contributor.authorEssen, Lars-Oliver
dc.date.accessioned2021-12-23T16:11:54Z-
dc.date.available2021-12-23T16:11:54Z-
dc.date.issued2018
dc.identifier.issn00318655
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/9945-
dc.description.abstractAll light-sensitive members of the photolyase/cryptochrome family rely on FAD as catalytic cofactor. Its activity is regulated by photoreduction, a light-triggered electron transfer process from a conserved tryptophan triad to the flavin. The stability of the reduced flavin depends on available external electron donors and oxygen. In this study, we show for the class II photolyase of Methanosarcina mazei, MmCPDII, that it utilizes physiologically relevant redox cofactors NADH and NADPH for the formation of the semiquinoid FAD in a light-dependent reaction. Using redox-inert variants MmCPDII/W388F and MmCPDII/W360F, we demonstrate that photoreduction by NADH and NADPH requires the class II-specific tryptophan cascade of MmCPDII. Finally, we confirmed that mutations in the tryptophan cascade can be introduced without any substantial structural disturbances by analyzing crystal structures of MmCPDII/W388F, MmCPDII/W360F and MmCPDII/Y345F.
dc.description.sponsorshipLOEWE Center SYNMIKRO (Center for Synthetic Microbiology, Hessen); Air Force Office of Scientific Research (AFOSR)United States Department of DefenseAir Force Office of Scientific Research (AFOSR) [FA9550-14-1-0409]; This work was funded by the LOEWE Center SYNMIKRO (Center for Synthetic Microbiology, Hessen) and by the Air Force Office of Scientific Research (AFOSR; grant FA9550-14-1-0409). We would like to thank Marian Vogt for helpful discussion, Ankan Banerjee for critical reading of the manuscript and the beamline staff of BL14.1 at the BESSYII (Berlin, Germany) and ID29 at the European Synchrotron Radiation Facility (ESRF Grenoble, France) for support during data collection.
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofPHOTOCHEMISTRY AND PHOTOBIOLOGY
dc.subjectARABIDOPSIS CRYPTOCHROME
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectELECTRON-TRANSFER
dc.subjectPHOTORECEPTOR
dc.subjectSITE
dc.titleNicotinamide Adenine Dinucleotides Arrest Photoreduction of Class II DNA Photolyases in FADH(center dot) State
dc.typejournal article
dc.identifier.doi10.1111/php.12834
dc.identifier.isiISI:000422743500009
dc.description.volume94
dc.description.issue1
dc.description.startpage81
dc.description.endpage87
dc.contributor.orcid0000-0003-4272-4026
dc.contributor.researcheridL-3862-2016
dc.identifier.eissn17511097
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationPhotochem. Photobiol.
dcterms.oaStatusBronze
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