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Photophysics of deinoxanthin, the keto-carotenoid bound to the main S-layer unit of Deinococcus radiodurans

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901162" target="_blank" >RIV/60076658:12310/20:43901162 - isvavai.cz</a>

  • Alternative codes found

    RIV/60077344:_____/20:00532606

  • Result on the web

    <a href="https://pubs.rsc.org/en/content/articlelanding/2020/pp/d0pp00031k/unauth#!divAbstract" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2020/pp/d0pp00031k/unauth#!divAbstract</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/d0pp00031k" target="_blank" >10.1039/d0pp00031k</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Photophysics of deinoxanthin, the keto-carotenoid bound to the main S-layer unit of Deinococcus radiodurans

  • Original language description

    The keto-carotenoid deinoxanthin, which occurs in the UV-resistant bacterium Deinococcus radiodurans, has been investigated by ultrafast time-resolved spectroscopy techniques. We have explored the excited-state properties of deinoxanthin in solution and bound to the S-layer Deinoxanthin Binding Complex (SDBC), a protein complex important for UV resistance and thermostability of the organism. Binding of deinoxanthin to SDBC shifts the absorption spectrum to longer wavelengths, but excited-state dynamics remain unaffected. The lifetime of the lowest excited state (S-1) of isolated deinoxanthin in methanol is 2.1 ps. When bound to SDBC, the S-1 lifetime is 2.4 ps, indicating essentially no alteration of the effective conjugation length upon binding. Moreover, our data show that the conformational disorder in both ground and excited states is the same for deinoxanthin in methanol and bound to SDBC. Our results thus suggest a rather loosely bound carotenoid in SDBC, making it very distinct from other carotenoid-binding proteins such as Orange Carotenoid Protein (OCP) or crustacyanin, both of which significantly restrain the carotenoid at the binding site. Three deinoxanthin analogs were found to bind the SDBC, suggesting a non-selective binding site of deinoxanthin in SDBC.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

    <a href="/en/project/GX19-28323X" target="_blank" >GX19-28323X: Relation between structure and function of carotenoids: New pathways to answer unresolved questions</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Photochemical &amp; Photobiological Sciences

  • ISSN

    1474-905X

  • e-ISSN

  • Volume of the periodical

    19

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

    495-503

  • UT code for WoS article

    000527017100007

  • EID of the result in the Scopus database

    2-s2.0-85083468400