Characterization of a 41 kDa photoinhibition adduct in isolated photosystem II reaction centres

Roberto Barbato; Giulia Friso; Fernanda Rigoni; Annalisa Frizzo; Giorgio M. Giacometti

doi:10.1016/0014-5793(92)81087-3

Characterization of a 41 kDa photoinhibition adduct in isolated photosystem II reaction centres

Roberto Barbato, Giulia Friso, Fernanda Rigoni, Annalisa Frizzo, Giorgio M. Giacometti

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

When isolated reaction centres of photosystem II are subjected to photoinhibitory illumination, a 41 kDa SDS-PAGE band is observed under all experimental conditions. The same band is also found, together will lower molecular weight fragments of the D1 protein, in whole thylakoids and in all PSII sub-particles investigated up to now. In the case of isolated reaction centres the 41 kDa band is represented by a heterodimer of the D1 polypeptide and the α-subunit of cytochrome b₅₅₉. The cross-linkage between D1 and α-cyl b₅₅₉ involves a region on D1 between the N-terminal residue and Arg·225, and is an early event in photo-induced damage to the D1 protein.

Lingua originale	Inglese
pagine (da-a)	165-169
Numero di pagine	5
Rivista	FEBS Letters
Volume	309
Numero di pubblicazione	2
DOI	https://doi.org/10.1016/0014-5793(92)81087-3
Stato di pubblicazione	Pubblicato - 7 set 1992
Pubblicato esternamente	Sì

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10.1016/0014-5793(92)81087-3

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@article{cb27b47e4b2b471e855e67fd4f2a8a54,

title = "Characterization of a 41 kDa photoinhibition adduct in isolated photosystem II reaction centres",

abstract = "When isolated reaction centres of photosystem II are subjected to photoinhibitory illumination, a 41 kDa SDS-PAGE band is observed under all experimental conditions. The same band is also found, together will lower molecular weight fragments of the D1 protein, in whole thylakoids and in all PSII sub-particles investigated up to now. In the case of isolated reaction centres the 41 kDa band is represented by a heterodimer of the D1 polypeptide and the α-subunit of cytochrome b559. The cross-linkage between D1 and α-cyl b559 involves a region on D1 between the N-terminal residue and Arg·225, and is an early event in photo-induced damage to the D1 protein.",

keywords = "Cytochrome b, D1 protein, Photoinhibition: Reaction centre, Photosystem II",

author = "Roberto Barbato and Giulia Friso and Fernanda Rigoni and Annalisa Frizzo and Giacometti, {Giorgio M.}",

note = "Funding Information: ~rdrrra~r~lril~cnlrnnrx: Pun of llic cost of this work WYSc crvcrcdb y the 40% progmm {\textquoteleft}Llvcprotein{\textquoteright} uf the Iloiiun Nrtionul Ministry of Rc-#wcI~(MURST),",

year = "1992",

month = sep,

day = "7",

doi = "10.1016/0014-5793(92)81087-3",

language = "English",

volume = "309",

pages = "165--169",

journal = "FEBS Letters",

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publisher = "John Wiley and Sons Inc.",

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TY - JOUR

T1 - Characterization of a 41 kDa photoinhibition adduct in isolated photosystem II reaction centres

AU - Barbato, Roberto

AU - Friso, Giulia

AU - Rigoni, Fernanda

AU - Frizzo, Annalisa

AU - Giacometti, Giorgio M.

N1 - Funding Information: ~rdrrra~r~lril~cnlrnnrx: Pun of llic cost of this work WYSc crvcrcdb y the 40% progmm ‘Llvcprotein’ uf the Iloiiun Nrtionul Ministry of Rc-#wcI~(MURST),

PY - 1992/9/7

Y1 - 1992/9/7

N2 - When isolated reaction centres of photosystem II are subjected to photoinhibitory illumination, a 41 kDa SDS-PAGE band is observed under all experimental conditions. The same band is also found, together will lower molecular weight fragments of the D1 protein, in whole thylakoids and in all PSII sub-particles investigated up to now. In the case of isolated reaction centres the 41 kDa band is represented by a heterodimer of the D1 polypeptide and the α-subunit of cytochrome b559. The cross-linkage between D1 and α-cyl b559 involves a region on D1 between the N-terminal residue and Arg·225, and is an early event in photo-induced damage to the D1 protein.

AB - When isolated reaction centres of photosystem II are subjected to photoinhibitory illumination, a 41 kDa SDS-PAGE band is observed under all experimental conditions. The same band is also found, together will lower molecular weight fragments of the D1 protein, in whole thylakoids and in all PSII sub-particles investigated up to now. In the case of isolated reaction centres the 41 kDa band is represented by a heterodimer of the D1 polypeptide and the α-subunit of cytochrome b559. The cross-linkage between D1 and α-cyl b559 involves a region on D1 between the N-terminal residue and Arg·225, and is an early event in photo-induced damage to the D1 protein.

KW - Cytochrome b

KW - D1 protein

KW - Photoinhibition: Reaction centre

KW - Photosystem II

UR - http://www.scopus.com/inward/record.url?scp=0026785175&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(92)81087-3

DO - 10.1016/0014-5793(92)81087-3

M3 - Article

SN - 0014-5793

VL - 309

SP - 165

EP - 169

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Characterization of a 41 kDa photoinhibition adduct in isolated photosystem II reaction centres

Abstract

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