Identification of the chromophores involved in aggregation-dependent energy quenching of the monomeric photosystem II antenna protein Lhcb5

Journal of Biological Chemistry

Volumn 285, Issue 36, 2010, Pages 28309-28321

  Ballottari, Matteo ^a   Girardon, Julien ^a   Betterle, Nico ^a   Morosinotto, Tomas ^b   Bassi, Roberto ^a  

^a UNIVERSITY OF VERONA   (Italy)

^b UNIVERSITY OF PADOVA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ANTENNAS; CHARGE TRANSFER; CHLOROPHYLL; CHROMOPHORES; HARVESTING; ION EXCHANGE; MASS TRANSFER; PLANTS (BOTANY); PORPHYRINS; PROTEINS; QUENCHING;

ANTENNA PROTEINS; ENERGY QUENCHING; HIGHER PLANTS; IN-VITRO; IN-VIVO; LIGHT ENERGY; LIGHT-HARVESTING COMPLEX II; NON-PHOTOCHEMICAL QUENCHING; PHOTOSYNTHETIC LIGHT; PHOTOSYSTEM II; SPECTROSCOPIC FEATURES; ZEAXANTHIN;

ENERGY HARVESTING;

CHLOROPHYLL; MEMBRANE PROTEIN; PROTEIN LHCB; UNCLASSIFIED DRUG; XANTHOPHYLL; ZEAXANTHIN; ARABIDOPSIS PROTEIN; CHLOROPHYLL A; CHLOROPHYLL BINDING PROTEIN; LHCB5 PROTEIN, ARABIDOPSIS; LIGHT HARVESTING SYSTEM; PHOTOSYSTEM II; PROTEIN SUBUNIT;

ARTICLE; BINDING SITE; CONTROLLED STUDY; LIGHT HARVESTING SYSTEM; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; ARABIDOPSIS; CHEMISTRY; ENERGY METABOLISM; GENETICS; METABOLISM; MUTAGENESIS; MUTATION; PHOTOSYSTEM II; PIGMENTATION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN RENATURATION; PROTEIN SUBUNIT; SPECTROFLUOROMETRY; TIME;

EMBRYOPHYTA;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; CHLOROPHYLL; CHLOROPHYLL BINDING PROTEINS; ENERGY METABOLISM; LIGHT-HARVESTING PROTEIN COMPLEXES; MUTAGENESIS; MUTATION; PHOTOSYSTEM II PROTEIN COMPLEX; PIGMENTATION; PROTEIN MULTIMERIZATION; PROTEIN RENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; SPECTROMETRY, FLUORESCENCE; TIME FACTORS; XANTHOPHYLLS; ZEAXANTHINS;

EID: 77956249596     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.124115     Document Type: Article

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