A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome

An animal-like cryptochrome derived from Chlamydomonas reinhardtii (CraCRY) is a bifunctional flavoenzyme harboring flavin adenine dinucleotide (FAD) as a photoreceptive/catalytic center and functions both in the regulation of gene transcription and the repair of UV-induced DNA lesions in a light-de...

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Autores principales: Hosokawa, Yuhei, Morita, Hiroyoshi, Nakamura, Mai, Yamamoto, Junpei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10551024/
https://www.ncbi.nlm.nih.gov/pubmed/37794070
http://dx.doi.org/10.1038/s41598-023-43930-0
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author Hosokawa, Yuhei
Morita, Hiroyoshi
Nakamura, Mai
Yamamoto, Junpei
author_facet Hosokawa, Yuhei
Morita, Hiroyoshi
Nakamura, Mai
Yamamoto, Junpei
author_sort Hosokawa, Yuhei
collection PubMed
description An animal-like cryptochrome derived from Chlamydomonas reinhardtii (CraCRY) is a bifunctional flavoenzyme harboring flavin adenine dinucleotide (FAD) as a photoreceptive/catalytic center and functions both in the regulation of gene transcription and the repair of UV-induced DNA lesions in a light-dependent manner, using different FAD redox states. To address how CraCRY stabilizes the physiologically relevant redox state of FAD, we investigated the thermodynamic and kinetic stability of the two-electron reduced anionic FAD state (FADH(−)) in CraCRY and related (6–4) photolyases. The thermodynamic stability of FADH(−) remained almost the same compared to that of all tested proteins. However, the kinetic stability of FADH(−) varied remarkably depending on the local structure of the secondary pocket, where an auxiliary chromophore, 8-hydroxy-7,8-didemethyl-5-deazariboflavin (8-HDF), can be accommodated. The observed effect of 8-HDF uptake on the enhancement of the kinetic stability of FADH(−) suggests an essential role of 8-HDF in the bifunctionality of CraCRY.
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spelling pubmed-105510242023-10-06 A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome Hosokawa, Yuhei Morita, Hiroyoshi Nakamura, Mai Yamamoto, Junpei Sci Rep Article An animal-like cryptochrome derived from Chlamydomonas reinhardtii (CraCRY) is a bifunctional flavoenzyme harboring flavin adenine dinucleotide (FAD) as a photoreceptive/catalytic center and functions both in the regulation of gene transcription and the repair of UV-induced DNA lesions in a light-dependent manner, using different FAD redox states. To address how CraCRY stabilizes the physiologically relevant redox state of FAD, we investigated the thermodynamic and kinetic stability of the two-electron reduced anionic FAD state (FADH(−)) in CraCRY and related (6–4) photolyases. The thermodynamic stability of FADH(−) remained almost the same compared to that of all tested proteins. However, the kinetic stability of FADH(−) varied remarkably depending on the local structure of the secondary pocket, where an auxiliary chromophore, 8-hydroxy-7,8-didemethyl-5-deazariboflavin (8-HDF), can be accommodated. The observed effect of 8-HDF uptake on the enhancement of the kinetic stability of FADH(−) suggests an essential role of 8-HDF in the bifunctionality of CraCRY. Nature Publishing Group UK 2023-10-04 /pmc/articles/PMC10551024/ /pubmed/37794070 http://dx.doi.org/10.1038/s41598-023-43930-0 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Hosokawa, Yuhei
Morita, Hiroyoshi
Nakamura, Mai
Yamamoto, Junpei
A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome
title A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome
title_full A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome
title_fullStr A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome
title_full_unstemmed A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome
title_short A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome
title_sort deazariboflavin chromophore kinetically stabilizes reduced fad state in a bifunctional cryptochrome
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10551024/
https://www.ncbi.nlm.nih.gov/pubmed/37794070
http://dx.doi.org/10.1038/s41598-023-43930-0
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