Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 532614
Title On the quantitative relation between dark kinetics of NPQ-induced changes in variable fluorescence and the activation state of the CF0·CF1·ATPase in leaves
Author(s) Vredenberg, W.J.
Source Photosynthetica 56 (2018)1. - ISSN 0300-3604 - p. 139 - 149.
DOI http://dx.doi.org/10.1007/s11099-018-0772-1
Department(s) Laboratory of Plant Physiology
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) CF·F·ATPase - chlorophyll fluorescence kinetics - Kautsky fluorescence induction curve - nonphotochemical quenching - quenching mechanisms - system analysis.
Abstract The variable fluorescence at the maximum Fm of the fluorescence induction (Kautsky) curve is known to be substantially suppressed shortly after light adaption due to nonphotochemical qE quenching. The kinetic pattern of the dark decay at Fm consists of three components with rates ~20, ~1, and ~0.1 s–1, respectively. Light adaptation has no or little effect on these rate constants. It causes a decrease in the ratio between the amplitudes of the slow and fast one with negligible change in the small amplitude of the ultra-slow component. Results add to evidence for the hypothesis that the dark-reversible decrease in variable fluorescence accompanying light adaptation during the P–S phase of the fluorescence induction curve is due to an alteration in nonphotochemical qE quenching caused by changes in the trans-thylakoid proton motive force in response to changes in the proton conductance gH+ of the CF0-channel of the CF0·CF1·ATPase.
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