Oxygen-evolving Complex Of Photosystem Research Articles

Sequence Similarity in Nuclear and Mitochondrial Gene Regions in Plants

A 114-basepair fragment at 5′-upstream of the gene oee2-A from Nicotiana tabacum encoding the 23kD polypeptide of oxygen-evolving complex of photosystem II was found, through database search, to have high sequence similarity with segments in the mitochondrial genome of Oenothera, watermelon and wheat. This observation is supported by the Southern hybridization data. Repeated sequences were also found in the nuclear-mitochondrial homologous region, However, the function of these repeats is yet to be determined.

Investigation of the origin of the "S3" EPR signal from the oxygen-evolving complex of photosystem 2: the role of tyrosine Z.

The origin of the "S3" EPR signal from calcium-depleted photosystem 2 samples has been investigated. This signal is observed after freezing samples under illumination and has been assigned to an interaction between the manganese cluster and an oxidized histidine radical [Boussac et al. (1990) Nature 347; 303-306]. In calcium-depleted samples prepared by three different methods, we observed the trapping of the tyrosine radical YZ+ under conditions which also formed the "S3" signal. An "S3"-type signal and YZ+ were also formed in PS2 samples treated with the water analogue ammonia. Following illumination at 277 K, the "S3" and YZ+ signals decayed at the same rate at 273 K in the dark. Both the YZ+ and "S3" signals decayed on storage at 77 K and could be subsequently regenerated by illumination at 8-77 K. No evidence to support histidine oxidation was found. The effects of DCMU, chelators, and alkaline pH on the dark-stable multiline S2 and the "S3" signals from calcium-depleted samples were determined. Both signals required the presence of EGTA or citrate for maximum yield. The addition of DCMU caused a reduction in the yield of "S3" generated by freezing under illumination. Incubation at pH 7.5 resulted in the loss of both signals. We propose that a variety of treatments which affect calcium and chloride binding cause a stabilization of the S2 state and slow the reduction of YZ+. This allows the trapping of YZ+, the interaction with the manganese cluster (probably in the S2 state) resulting in the "S3" signal. The data allow the position of the manganese cluster to be estimated as within 10 A of tyrosine Z (D1-161).

Changes in the activity and the polypeptide composition of the oxygen-evolving complex in photosystem II of tobacco leaves infected with cucumber mosaic virus strain Y.

The amount of 22- and 23-kDa polypeptides in a 23-kDa protein family, which plays a regulatory role in photosynthetic oxygen evolution, decreased significantly during the progress of appearance of chlorotic spots in cucumber mosaic virus strain Y (CMV[Y])-inoculated tobacco (Nicotiana tabacum 'Ky57') leaves (Plant Mol. Biol. 16:689-698, 1991). The present study was conducted to determine if the amount of other polypeptides of the oxygen-evolving complex and the oxygen-evolving activity also decreased in CMV(Y)-inoculated tobacco leaves. The amount of a 33-kDa polypeptide, which is essential to oxygen evolution, did not decrease in CMV(Y)-inoculated leaves showing early symptoms, although the amount of 22- and 23-kDa polypeptides began to decrease. However, comparative analysis of electron transport in thylakoid membranes indicated that the oxygen-evolving activity in CMV(Y)-inoculated tobacco leaves was only partly reduced, compared with the activity in CMV(O)-inoculated tobacco leaves which did not show clear symptoms. Partial inhibition of the oxygen-evolving activity, by a differential decrease in the amount of polypeptides of the oxygen-evolving complex, seems to be associated with the primary molecular process of symptom expression in CMV(Y)-inoculated tobacco leaves.

A protein in the oxygen-evolving complex in the chloroplast is associated with symptom expression on tobacco leaves infected with cucumber mosaic virus strain Y

To elucidate the molecular basis of symptom expression in virus-infected plants, the changes in proteins between tobacco, Nicotiana tabacum cv. Ky57, leaves inoculated with cucumber mosaic virus strain Y [CMV(Y)] and strain O [CMV(O)], were compared by 2-dimensional (2-D) gel electrophoresis. The appearance of chlorotic spots in CMV(Y)-inoculated tobacco leaves accompanied an increase of 3 polypeptides and a decrease in 6 polypeptides, as compared with those in the CMV(O)-inoculated tobacco which showed no clear symptoms. The decrease in the amounts of two polypeptides of 22 and 23 kDa was particularly significant: these two polypeptides were compared with a 24 kDa polypeptide, which co-migrated with them in 2-D gel electrophoresis but did not clearly decrease at an early stage of infection, as well as major other proteins of CMV(Y)-inoculated tobacco leaves. However, the 22, 23 and 24 kDa polypeptides showed the same peptide mapping pattern. Furthermore, the 12 amino acid residues at N-termini of the three polypeptides match those of the extrinsic 23 kDa polypeptide of an oxygen-evolving complex from spinach. A comparative analysis of the 22, 23 and 24 kDa polypeptides in N. tabacum and its ancestral parents, N. sylvestris and N. tomentosiformis, revealed that the 22 kDa polypeptide derives from N. sylvestris and the 23 kDa polypeptide from N. tomentosiformis; the 24 kDa polypeptide derives from both ancestral Nicotiana species. The results indicate that the polypeptides whose amounts differentially decrease with the progress of symptom expression in N. tabacum inoculated with CMV(Y) are one component of the oxygen-evolving complex in photosystem II.

The microwave power saturation of SIIslow varies with the redox state of the oxygen-evolving complex in photosystem II

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe microwave power saturation of SIIslow varies with the redox state of the oxygen-evolving complex in photosystem IIStenbjoern A. Styring and A. William RutherfordCite this: Biochemistry 1988, 27, 13, 4915–4923Publication Date (Print):June 28, 1988Publication History Published online1 May 2002Published inissue 28 June 1988https://doi.org/10.1021/bi00413a049RIGHTS & PERMISSIONSArticle Views120Altmetric-Citations82LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (1 MB) Get e-Alerts Get e-Alerts

Deactivation kinetics and temperature dependence of the S-state transitions in the oxygen-evolving system of Photosystem II measured by EPR spectroscopy

The decay kinetics for the S 2 and S 3 states of the oxygen-evolving complex in Photosystem II have been measured in the presence of an external electron acceptor. The S 2- and S 3-states decay monophasically with half-decay times at 18°C of 3–3.5 min and 3.5–4 min, respectively. The results also show that S 3 decays via S 2 under these circumstances. The temperature dependence of the individual S-state transitions has been measured in single flash experiments in which the multiline EPR signal originating from the S 2 state has been used as spectroscopic probe. The half-inhibition temperatures are for S 0 to S 1 220–225 K, for S 1 to S 2 135–140 K, for S 2 to S 3 230 K and for the S 3-to-S 0 transition 235 K.

Protection of photosynthetic O2 evolution against heat inactivation: the role of chloride, pH and coupling status

Heat inactivation of photosynthetic O2 evolution was studied in isolated thylakoids from spinach (Spinacia oleracea) and mangrove (Avicennia marina) leaves. Different temperatures, salt, pH and uncoupler effects were investigated. From these results and others in the literature it was concluced that chloride loss from the membrane and, more specifically, the oxygen-evolving complex of photosystem II, may be the cause of inhibition of oxygen evolution during heat inactivation.

Polypeptides of the oxygen-evolving complex of Photosystem II in cyanobacteria

Polypeptides of the oxygen-evolving complex of Photosystem II in cyanobacteria

Destabilization by high pH of the S 1-state of the oxygen-evolving complex in photosystem II particles

The S-state distribution in a dark-adapted photosystem II preparation, isolated from spinach chloroplasts, can be changed by pH. The period 4 oscillation of the oxygen-releasing reaction, as measured by UV absorbance changes, is shifted by one flash at pH 8.3. This is not due to the generation of the EPR signal II on the first flash, or to the loss of a positive charge to some other electron donor after the first flashes. It is concluded that at pH 8.3 the S 1-state is reduced to S 0. The half-time of the reduction of S 1 to S 0 is 45 s, and the reduction is reversed in the dark if the pH is readjusted to pH 6.0. The oxygen release at pH 8.3 is irreversibly slowed down to about 3.2 ms.