期刊
PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES
卷 21, 期 4, 页码 493-507出版社
SPRINGERNATURE
DOI: 10.1007/s43630-022-00214-2
关键词
BLUF proteins; Photosensor; Reaction; Diffusion; Transient grating
资金
- MEXT/JSPS [JP20107003, JP25102004, 17H03008, 21H01885, 21K19218, 18H045522, 20H04708]
- Grants-in-Aid for Scientific Research [21H01885, 21K19218, 20H04708] Funding Source: KAKEN
This review describes the reactions of three BLUF proteins with similar EAL functional groups or with a separated target protein using time-resolved diffusion technique.
BLUF (blue light sensor using flavin) proteins are the blue light receptors that consist of flavin-binding BLUF domains and functional domains. Upon blue light excitation, the hydrogen bond network around the flavin chromophore changes, and the absorption spectrum in the visible region shifts to red. Light signal received in the BLUF domain is intramolecularly or intermolecularly transmitted to the functional region. In this review, the reactions of three BLUF proteins with similar EAL functional groups within the protein (BlrP1, and YcgF), or with a separated target protein (PapB) are described using time-resolved diffusion technique. The diffusion coefficients (D) of the BLUF domains did not significantly change upon photoexcitation, whereas those of the full-length proteins BlrP1 and YcgF and the PapB-PapA system significantly decreased. The changes in D should be due to diffusion-sensitive conformational changes (DSCC) that alter the friction of diffusion. The time constants of the major D changes of BlrP1 and PapB-PapA were similar (similar to 20 ms), although the magnitude of the friction change depended on the proteins. Similarities and differences among the reactions of these proteins were clarified from the viewpoint of DSCC. [GRAPHICS] .
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