QA Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II

Wim Vermaas, Jeroen Charité, Gaozhong Shen

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Two D2 mutants were created with a site-directed mutation near the presumable binding site of QA. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to QAand/or in binding of QA, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photoheterotroph. In another mutant the Gly-215 residue, located next to the His residue that is proposed to bind QA and Fe2+, was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction centers on a chlorophyll basis. We propose that proper binding of QA to the photosystem II reaction center complex is a prerequisite for stability of the photosystem II complex. Impairment of QA binding leads to rapid inactivation of photosystem II, which may be followed by a structural disintegration of the complex.

Original languageEnglish (US)
Pages (from-to)359-365
Number of pages7
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume45
Issue number5
DOIs
StatePublished - Jan 1 1990

Fingerprint

Photosystem II Protein Complex
Structural integrity
Pheophytins
Mutation
Thylakoids
Disintegration
Chlorophyll
Electron Transport
Binding Sites
Oxygen
Light

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

@article{4c5afeb1a84f483ebfffa7b9f7f0a681,
title = "QA Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II",
abstract = "Two D2 mutants were created with a site-directed mutation near the presumable binding site of QA. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to QAand/or in binding of QA, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photoheterotroph. In another mutant the Gly-215 residue, located next to the His residue that is proposed to bind QA and Fe2+, was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction centers on a chlorophyll basis. We propose that proper binding of QA to the photosystem II reaction center complex is a prerequisite for stability of the photosystem II complex. Impairment of QA binding leads to rapid inactivation of photosystem II, which may be followed by a structural disintegration of the complex.",
author = "Wim Vermaas and Jeroen Charit{\'e} and Gaozhong Shen",
year = "1990",
month = "1",
day = "1",
doi = "10.1515/znc-1990-0509",
language = "English (US)",
volume = "45",
pages = "359--365",
journal = "Zeitschrift fur Naturforschung - Section C Journal of Biosciences",
issn = "0939-5075",
publisher = "Verlag der Zeitschrift fur Naturforschung",
number = "5",

}

QA Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II. / Vermaas, Wim; Charité, Jeroen; Shen, Gaozhong.

In: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Vol. 45, No. 5, 01.01.1990, p. 359-365.

Research output: Contribution to journalArticle

TY - JOUR

T1 - QA Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II

AU - Vermaas, Wim

AU - Charité, Jeroen

AU - Shen, Gaozhong

PY - 1990/1/1

Y1 - 1990/1/1

N2 - Two D2 mutants were created with a site-directed mutation near the presumable binding site of QA. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to QAand/or in binding of QA, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photoheterotroph. In another mutant the Gly-215 residue, located next to the His residue that is proposed to bind QA and Fe2+, was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction centers on a chlorophyll basis. We propose that proper binding of QA to the photosystem II reaction center complex is a prerequisite for stability of the photosystem II complex. Impairment of QA binding leads to rapid inactivation of photosystem II, which may be followed by a structural disintegration of the complex.

AB - Two D2 mutants were created with a site-directed mutation near the presumable binding site of QA. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to QAand/or in binding of QA, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photoheterotroph. In another mutant the Gly-215 residue, located next to the His residue that is proposed to bind QA and Fe2+, was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction centers on a chlorophyll basis. We propose that proper binding of QA to the photosystem II reaction center complex is a prerequisite for stability of the photosystem II complex. Impairment of QA binding leads to rapid inactivation of photosystem II, which may be followed by a structural disintegration of the complex.

UR - http://www.scopus.com/inward/record.url?scp=84945025470&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84945025470&partnerID=8YFLogxK

U2 - 10.1515/znc-1990-0509

DO - 10.1515/znc-1990-0509

M3 - Article

VL - 45

SP - 359

EP - 365

JO - Zeitschrift fur Naturforschung - Section C Journal of Biosciences

JF - Zeitschrift fur Naturforschung - Section C Journal of Biosciences

SN - 0939-5075

IS - 5

ER -