مورد إلكتروني
Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase
| العنوان: | Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase |
|---|---|
| بيانات النشر: | National Academy of Sciences 2017 |
| تفاصيل مُضافة: | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular Ministerio de Economia, Industria y Competitividad (MINECO). España Buey, Rubén M. Arellano, Juan B. López Maury, Luis Galindo Trigo, Sergio Velázquez Campoy, Adrián Revuelta, José Luis Pereda, José M. de Florencio Bellido, Francisco Javier Schürmann, Peter Buchanan, Bob B. Balsera, Monica |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | Flavoproteinsparticipateinawidevarietyofphysiologicallyrelevant processes that typically involve redox reactions. Within this protein superfamily, there exists a group that is able to transfer reducing equivalents from FAD to a redox-active disulfide bridge, which further reduces disulfide bridges in target proteins to regulate their structure and function. We have identified a previously undescribed type of flavin enzyme that is exclusive to oxygenic photosynthetic prokaryotes and that is based on the primary sequence that had been assigned as an NADPH-dependent thioredoxin reductase (NTR). However, our experimental data show that the protein does not transfer reducing equivalents from flavins to disulfides as in NTRs but functions in the opposite direction. High-resolution structures of the protein from Gloeobacter violaceus and Synechocystis sp. PCC6803 obtained by X-ray crystallography showed two juxtaposed FADmoleculespermonomerinredoxcommunicationwithanactive disulfide bridge in a variant of the fold adopted by NTRs. We have tentatively named the flavoprotein “DDOR” (diflavin-linked disulfide oxidoreductase) and propose that its activity is linked to a thiol-basedtransferofreducingequivalentsinbacterialmembranes. These findings expand the structural and mechanistic repertoire of flavoenzymes with oxidoreductase activity and pave the way to explore new protein engineering approaches aimed at designing redox-active proteins for diverse biotechnological applications. |
| مصطلحات الفهرس: | Flavoprotein, Transfer of reducing equivalents, Redox active disulfide, Rossmann fold, Sulfhydry, info:eu-repo/semantics/article |
| URL: | Proceedings of the National Academy of Sciences, 114 (48), 12725-12730. BFU2016-80343-P BIO2016-75634-P |
| الإتاحة: | Open access content. Open access content http://creativecommons.org/licenses/by-nc-nd/4.0 info:eu-repo/semantics/openAccess Attribution-NonCommercial-NoDerivatives 4.0 Internacional |
| ملاحظة: | English |
| أرقام أخرى: | SUE oai:idus.us.es:11441/98976 Buey, R.M., Arellano, J.B., López Maury, L., Galindo Trigo, S., Velázquez Campoy, A., Revuelta, J.L.,...,Balsera, M. (2017). Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase. Proceedings of the National Academy of Sciences, 114 (48), 12725-12730. 0027-8424 (impreso) 1091-6490 (electrónico) 10.1073/pnas.1713698114 1410773579 |
| المصدر المساهم: | UNIV DE SEVILLA From OAIster®, provided by the OCLC Cooperative. |
| رقم الأكسشن: | edsoai.on1410773579 |
| قاعدة البيانات: | OAIster |
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