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1.
Biochemistry ; 34(35): 11133-41, 1995 Sep 05.
Artigo em Inglês | MEDLINE | ID: mdl-7669771

RESUMO

An intrinsic 22 kDa protein of photosystem II has been shown to possess high sequence homology with the CAB gene products, but differs from these proteins by an additional putative fourth transmembrane helix. This protein, designated PSII-S in accordance with the assignment of the name psbS to its gene, has been isolated by nonionic detergents and preparative isoelectric focusing in this study. The isolated PSII-S protein was shown to bind 5 chlorophyll molecules (a and b) per protein unit and also several different kinds of carotenoids. The room temperature absorption spectrum of the Qy transition of the chlorophylls bound to the isolated protein is characterized by a broad band with a maximum at 671 nm. The 77 K fluorescence spectrum exhibits a peak at 672 nm. A single photon counting technique was applied to resolve the room temperature decay kinetics of the first excited singlet states in the chlorophyll ensemble of the PSII-S protein. The data can be satisfactorily described by triexponential kinetics with lifetimes of tau 1 = 1.8 ns, tau 2 = 4.4 ns, and tau 3 = 6.1 ns and normalized amplitudes of 0.09, 0.60, and 0.31, respectively. Circular dichroism spectra suggest that, in contrast to LHCII, virtually no pigment coupling exists in the PSII-S protein. Two copies of the PSII-S protein were found per PSII in spinach thylakoids. It displays an unusually extreme lateral heterogeneity, since the PSII beta centers located in the stroma exposed thylakoid regions contained only residual amounts of the PSII-S protein.(ABSTRACT TRUNCATED AT 250 WORDS)


Assuntos
Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Complexo de Proteína do Fotossistema II , Proteínas de Plantas , Proteínas de Transporte/química , Proteínas de Transporte/metabolismo , Clorofila/metabolismo , Complexos de Proteínas Captadores de Luz , Estrutura Molecular , Peso Molecular , Fotossíntese , Complexo de Proteínas do Centro de Reação Fotossintética/química , Pigmentos Biológicos/metabolismo , Ligação Proteica , Espectrometria de Fluorescência , Spinacia oleracea/química , Spinacia oleracea/metabolismo
2.
Photosynth Res ; 27(2): 97-108, 1991 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-24414573

RESUMO

Photoinhibition was analyzed in O2-evolving and in Tris-treated PS II membrane fragments by measuring flash-induced absorption changes at 830 nm reflecting the transient P680(+) formation and oxygen evolution. Irradiation by visible light affects the PS II electron transfer at two different sites: a) photoinhibition of site I eliminates the capability to perform a 'stable' charge separation between P680(+) and QA (-) within the reaction center (RC) and b) photoinhibition of site II blocks the electron transfer from YZ to P680(+). The quantum yield of site I photoinhibition (2-3×10(-7) inhibited RC/quantum) is independent of the functional integrity of the water oxidizing system. In contrast, the quantum yield of photoinhibition at site II depends strongly on the oxygen evolution capacity. In O2-evolving samples, the quantum yield of site II photoinhibition is about 10(-7) inhibited RC/quantum. After selective elimination of the O2-evolving capacity by Tris-treatment, the quantum yield of photoinhibition at site II depends on the light intensity. At low intensity (<3 W/m(2)), the quantum yield is 10(-4) inhibited RC/quantum (about 1000 times higher than in oxygen evolving samples). Based on these results it is inferred that the dominating deleterious effect of photoinhibition cannot be ascribed to an unique target site or a single mechanism because it depends on different experimental conditions (e.g., light intensity) and the functional status of the PS II complex.

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