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Light-induced reversible reorganizations in closed Type II reaction centre complexes: physiological roles and physical mechanisms

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17310%2F22%3AA2302HRC" target="_blank" >RIV/61988987:17310/22:A2302HRC - isvavai.cz</a>

  • Result on the web

    <a href="https://royalsocietypublishing.org/doi/10.1098/rsob.220297" target="_blank" >https://royalsocietypublishing.org/doi/10.1098/rsob.220297</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1098/rsob.220297" target="_blank" >10.1098/rsob.220297</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Light-induced reversible reorganizations in closed Type II reaction centre complexes: physiological roles and physical mechanisms

  • Original language description

    The purpose of this review is to outline our understanding of the nature, mechanism and physiological significance of light-induced reversible reorganizations in closed Type II reaction centre (RC) complexes. In the so-called ‘closed' state, purple bacterial RC (bRC) and photosystem II (PSII) RC complexes are incapable of generating additional stable charge separation. Yet, upon continued excitation they display well-discernible changes in their photophysical and photochemical parameters. Substantial stabilization of their charge-separated states has been thoroughly documented—uncovering light-induced reorganizations in closed RCs and revealing their physiological importance in gradually optimizing the operation of the photosynthetic machinery during the dark-to-light transition. A range of subtle light-induced conformational changes has indeed been detected experimentally in different laboratories using different bRC and PSII-containing preparations. In general, the presently available data strongly suggest similar structural dynamics of closed bRC and PSII RC complexes, and similar physical mechanisms, in which dielectric relaxation processes and structural memory effects of proteins are proposed to play important roles.

  • 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

    10610 - Biophysics

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Open Biology

  • ISSN

    2046-2441

  • e-ISSN

    2046-2441

  • Volume of the periodical

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    15

  • Pages from-to

    1-15

  • UT code for WoS article

    000898098200003

  • EID of the result in the Scopus database

    2-s2.0-85144144114