Hydrogen Bonding Environment of the N3-H Group of Flavin Mononucleotide in the Light Oxygen Voltage Domains of Phototropins
| Autor: | Atsushi Yamamoto, Takayuki Koyama, D. Nozaki, Kiyoshi Shiga, Tatsuya Iwata, Yasuzo Nishina, Satoru Tokutomi, Masashi Unno, Hideki Kandori |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Phototropins Phototropin 030102 biochemistry & molecular biology Chemistry Hydrogen bond Arabidopsis Proteins Flavin Mononucleotide Flavin mononucleotide chemistry.chemical_element Phot Hydrogen Bonding Photochemistry Biochemistry Oxygen DNA-Binding Proteins 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology Protein kinase domain Domain (ring theory) Biophysics Fourier transform infrared spectroscopy |
| Zdroj: | Biochemistry. 56(24) |
| ISSN: | 1520-4995 |
| Popis: | The light oxygen voltage (LOV) domain is a flavin-binding blue-light receptor domain, originally found in a plant photoreceptor phototropin (phot). Recently, LOV domains have been used in optogenetics as the photosensory domain of fusion proteins. Therefore, it is important to understand how LOV domains exhibit light-induced structural changes for the kinase domain regulation, which enables the design of LOV-containing optogenetics tools with higher photoactivation efficiency. In this study, the hydrogen bonding environment of the N3–H group of flavin mononucleotide (FMN) of the LOV2 domain from Adiantum neochrome (neo) 1 was investigated by low-temperature Fourier transform infrared spectroscopy. Using specifically 15N-labeled FMN, [1,3-15N2]FMN, the N3–H stretch was identified at 2831 cm–1 for the unphotolyzed state at 150 K, indicating that the N3–H group forms a fairly strong hydrogen bond. The N3–H stretch showed temperature dependence, with a shift to lower frequencies at ≤200 K and to higher freque... |
| Databáze: | OpenAIRE |
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