Phytochromes (Phys) are biliproteins that regulate light responses
in plants, fungi, and microorganisms through photoconversion
between a dark state and a photoproduct. Thermal
reversion of the photoproduct is an intrinsic property of all
Phys, typically occurring on a timescale of seconds to days.
Despite methodological advances, the structural and spectroscopic
determination of short-lived photoproducts has proven
challenging. We herein present an innovative approach for
photoproduct stabilisation by incorporating the protein into
trehalose glasses (TGs). The resulting Phy–trehalose matrices
were investigated by UV/Vis absorption and solid-state NMR
spectroscopies. Our results demonstrate that the TGs strongly
inhibit thermal reversion of the incorporated Phy proteins for
periods as long as several weeks at room temperature (RT),
during which the proteins fully sustain their native structures
and spectral and biochemical properties. This sample preparation
approach is beneficial for revealing bona fide structure/
function relationships of short-lived photoproducts that are
otherwise not accessible, thus paving the way towards a deeper
molecular understanding of the diversified spectral properties
of Phys. Our results also provide new insights into the molecular
mechanism of trehalose bioprotection.
| Identifer | oai:union.ndltd.org:DRESDEN/oai:qucosa:de:qucosa:86926 |
| Date | 28 August 2023 |
| Creators | Köhler, Lisa, Gärtner, Wolfgang, Matysik, Jörg, Song, Chen Song |
| Publisher | Wiley-VCH |
| Source Sets | Hochschulschriftenserver (HSSS) der SLUB Dresden |
| Language | English |
| Detected Language | English |
| Type | info:eu-repo/semantics/publishedVersion, doc-type:article, info:eu-repo/semantics/article, doc-type:Text |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | 10.1002/cptc.202100220 |
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