Histidine residue 252 of the Photosystem II D1 polypeptide is involved in a light-induced cross-linking of the polypeptide with the α subunit of cytochrome b-559: Study of a site-directed mutant of Synechocystis PCC 6803

Lenka Lupínková, James G. Metz, Bruce A. Diner, I. Vass, Josef Komenda

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Properties of the Photosystem II (PSII) complex were examined in the wild-type (control) strain of the cyanobacterium Synechocystis PCC 6803 and its site-directed mutant D1-His252Leu in which the histidine residue 252 of the D1 polypeptide was replaced by leucine. This mutation caused a severe blockage of electron transfer between the PSII electron acceptors QA and QB and largely inhibited PSII oxygen evolving activity. Strong illumination induced formation of a D1-cytochrome b-559 adduct in isolated, detergent-solubilized thylakoid membranes from the control but not the mutant strain. The light-induced generation of the adduct was suppressed after prior modification of thylakoid proteins either with the histidine modifier platinum-terpyridine-chloride or with primary amino group modifiers. Anaerobic conditions and the presence of radical scavengers also inhibited the appearance of the adduct. The data suggest that the D1-cytochrome adduct is the product of a reaction between the oxidized residue His252 of the D1 polypeptide and the N-terminal amino group of the cytochrome α subunit. As the rate of the D1 degradation in the control and mutant strains is similar, formation of the adduct does not seem to represent a required intermediary step in the D1 degradation pathway.

Original languageEnglish
Pages (from-to)192-201
Number of pages10
JournalBBA - Bioenergetics
Volume1554
Issue number3
DOIs
Publication statusPublished - Jul 1 2002

Fingerprint

Synechocystis
Photosystem II Protein Complex
Histidine
Thylakoids
Cytochromes
Light
Peptides
Electrons
Strain control
Degradation
Cyanobacteria
Platinum
Lighting
Leucine
Detergents
Chlorides
Oxygen
Membranes
Mutation
cytochrome b559

Keywords

  • Cyanobacterium
  • Cytochrome b-559
  • D1 polypeptide
  • Photoinhibition
  • Photosystem II
  • Synechocystis PCC 6803

ASJC Scopus subject areas

  • Biophysics

Cite this

Histidine residue 252 of the Photosystem II D1 polypeptide is involved in a light-induced cross-linking of the polypeptide with the α subunit of cytochrome b-559 : Study of a site-directed mutant of Synechocystis PCC 6803. / Lupínková, Lenka; Metz, James G.; Diner, Bruce A.; Vass, I.; Komenda, Josef.

In: BBA - Bioenergetics, Vol. 1554, No. 3, 01.07.2002, p. 192-201.

Research output: Contribution to journalArticle

@article{d6888227aced433c865c15f0dd0fa56c,
title = "Histidine residue 252 of the Photosystem II D1 polypeptide is involved in a light-induced cross-linking of the polypeptide with the α subunit of cytochrome b-559: Study of a site-directed mutant of Synechocystis PCC 6803",
abstract = "Properties of the Photosystem II (PSII) complex were examined in the wild-type (control) strain of the cyanobacterium Synechocystis PCC 6803 and its site-directed mutant D1-His252Leu in which the histidine residue 252 of the D1 polypeptide was replaced by leucine. This mutation caused a severe blockage of electron transfer between the PSII electron acceptors QA and QB and largely inhibited PSII oxygen evolving activity. Strong illumination induced formation of a D1-cytochrome b-559 adduct in isolated, detergent-solubilized thylakoid membranes from the control but not the mutant strain. The light-induced generation of the adduct was suppressed after prior modification of thylakoid proteins either with the histidine modifier platinum-terpyridine-chloride or with primary amino group modifiers. Anaerobic conditions and the presence of radical scavengers also inhibited the appearance of the adduct. The data suggest that the D1-cytochrome adduct is the product of a reaction between the oxidized residue His252 of the D1 polypeptide and the N-terminal amino group of the cytochrome α subunit. As the rate of the D1 degradation in the control and mutant strains is similar, formation of the adduct does not seem to represent a required intermediary step in the D1 degradation pathway.",
keywords = "Cyanobacterium, Cytochrome b-559, D1 polypeptide, Photoinhibition, Photosystem II, Synechocystis PCC 6803",
author = "Lenka Lup{\'i}nkov{\'a} and Metz, {James G.} and Diner, {Bruce A.} and I. Vass and Josef Komenda",
year = "2002",
month = "7",
day = "1",
doi = "10.1016/S0005-2728(02)00243-8",
language = "English",
volume = "1554",
pages = "192--201",
journal = "Biochimica et Biophysica Acta - Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Histidine residue 252 of the Photosystem II D1 polypeptide is involved in a light-induced cross-linking of the polypeptide with the α subunit of cytochrome b-559

T2 - Study of a site-directed mutant of Synechocystis PCC 6803

AU - Lupínková, Lenka

AU - Metz, James G.

AU - Diner, Bruce A.

AU - Vass, I.

AU - Komenda, Josef

PY - 2002/7/1

Y1 - 2002/7/1

N2 - Properties of the Photosystem II (PSII) complex were examined in the wild-type (control) strain of the cyanobacterium Synechocystis PCC 6803 and its site-directed mutant D1-His252Leu in which the histidine residue 252 of the D1 polypeptide was replaced by leucine. This mutation caused a severe blockage of electron transfer between the PSII electron acceptors QA and QB and largely inhibited PSII oxygen evolving activity. Strong illumination induced formation of a D1-cytochrome b-559 adduct in isolated, detergent-solubilized thylakoid membranes from the control but not the mutant strain. The light-induced generation of the adduct was suppressed after prior modification of thylakoid proteins either with the histidine modifier platinum-terpyridine-chloride or with primary amino group modifiers. Anaerobic conditions and the presence of radical scavengers also inhibited the appearance of the adduct. The data suggest that the D1-cytochrome adduct is the product of a reaction between the oxidized residue His252 of the D1 polypeptide and the N-terminal amino group of the cytochrome α subunit. As the rate of the D1 degradation in the control and mutant strains is similar, formation of the adduct does not seem to represent a required intermediary step in the D1 degradation pathway.

AB - Properties of the Photosystem II (PSII) complex were examined in the wild-type (control) strain of the cyanobacterium Synechocystis PCC 6803 and its site-directed mutant D1-His252Leu in which the histidine residue 252 of the D1 polypeptide was replaced by leucine. This mutation caused a severe blockage of electron transfer between the PSII electron acceptors QA and QB and largely inhibited PSII oxygen evolving activity. Strong illumination induced formation of a D1-cytochrome b-559 adduct in isolated, detergent-solubilized thylakoid membranes from the control but not the mutant strain. The light-induced generation of the adduct was suppressed after prior modification of thylakoid proteins either with the histidine modifier platinum-terpyridine-chloride or with primary amino group modifiers. Anaerobic conditions and the presence of radical scavengers also inhibited the appearance of the adduct. The data suggest that the D1-cytochrome adduct is the product of a reaction between the oxidized residue His252 of the D1 polypeptide and the N-terminal amino group of the cytochrome α subunit. As the rate of the D1 degradation in the control and mutant strains is similar, formation of the adduct does not seem to represent a required intermediary step in the D1 degradation pathway.

KW - Cyanobacterium

KW - Cytochrome b-559

KW - D1 polypeptide

KW - Photoinhibition

KW - Photosystem II

KW - Synechocystis PCC 6803

UR - http://www.scopus.com/inward/record.url?scp=0036649629&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036649629&partnerID=8YFLogxK

U2 - 10.1016/S0005-2728(02)00243-8

DO - 10.1016/S0005-2728(02)00243-8

M3 - Article

C2 - 12160992

AN - SCOPUS:0036649629

VL - 1554

SP - 192

EP - 201

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 3

ER -