Scavenging of superoxide generated in photosystem I by plastoquinol and other prenyllipids in thylakoid membranes.

We have examined scavenging of a superoxide by various prenyllipids occurring in thylakoid membranes, such as plastoquinone-9, alpha-tocopherolquinone, their reduced forms, and alpha-tocopherol, measuring oxygen uptake in hexane-extracted and untreated spinach thylakoids with a fast oxygen electrode under flash-light illumination. The obtained results demonstrated that all the investigated prenyllipids showed the superoxide scavenging properties, and plastoquinol-9 was the most active in this respect. Plastoquinol-9 formed in thylakoids as a result of enzymatic reduction of plastoquinone-9 by ferredoxin-plastoquinone reductase was even more active than the externally added plastoquinol-9 in the investigated reaction.

18O isotope effect in the photosynthetic water splitting process.

In mass spectroscopic experiments of oxygen evolution in Photosystem II at 50% enrichment of H(2)18O, one expects equal signals of 18O(2) and 16O(2) unless one of the isotopes is favored by the oxygen evolving complex (OEC). We have observed a deviation from this expectation, being a clear indication of an isotope effect. We have measured the effect to be 1.

Mössbauer studies of the non-heme iron and cytochrome b559 in a Chlamydomonas reinhardtii PSI- mutant and their interactions with alpha-tocopherol quinone.

Spin and valence states of the non-heme iron and the heme iron of cytochrome b559, as well as their interactions with alpha-tocopherol quinone (alpha-TQ) in photosystem II (PSII) thylakoid membranes prepared from the Chlamydomonas reinhardtii PSI- mutant have been studied using Mössbauer spectroscopy. Both of the iron atoms are in low spin ferrous states. The Debye temperature of the non-heme is 194 K and of the heme iron is 182 K.

Inhibition of oxygen evolution in Photosystem II by Cu(II) ions is associated with oxidation of cytochrome b559.

We have found that elevated copper concentrations, apart from the inhibition of oxygen evolution, changed the initial states distribution of the oxygen-evolving complex. Already at low concentrations, copper ions oxidized the low-potential form of cytochrome b (559) and also its high-potential form at higher concentrations at which fluorescence quenching was observed. We suggest that the primary target sites in Photosystem II for copper is tyrosine(z), both cytochrome b (559) forms and chlorophyll(z), and that these sites are the source of the copper-induced fluorescence quenching and oxygen evolution inhibition in Photosystem II.

Stimulation of oxygen evolution in photosystem II by copper(II) ions.

We have found that copper(II) ions at about equimolar Cu2+/photosystem II (PS II) reaction center proportions stimulate oxygen evolution nearly twofold. This high affinity Cu-binding site is different from the binding sites of Mn and Ca ions. The analysis of the Cu2+ content in PS II preparations isolated from wild-type tobacco and a tobacco mutant deficient in light-harvesting complex suggests that Cu2+ may be a native component of PS II and may take part in the oxygen evolution process.

Influence of different light intensities on the content of diosgenin, lipids, carotenoids and fatty acids in leaves of Dioscorea zingiberensis.

Cultivation of the climbing plant Dioscorea zingiberensis at a light intensity of 100 microE. m(-2) sec(-1) yields three different phenotypes. Most of the plants grow as green phenotype (DzW).