A. A. Khorobrykh

Interaction of molecular oxygen with the donor side of photosystem II after destruction of the water-oxidizing complex

Photosystem II (PSII) is a pigment-protein complex of thylakoid membrane of higher plants, algae, and cyanobacteria where light energy is used for oxidation of water and reduction of plastoquinone. Light-dependent reactions (generation of excited states of pigments, electron transfer, water oxidation) taking place in PSII can lead to the formation of reactive oxygen species. In this review attention is focused on the problem of interaction of molecular oxygen with the donor site of PSII, where after the removal of manganese from the water-oxidizing complex illumination induces formation of long-lived states (P680+· and TyrZ·) capable of oxidizing surrounding organic molecules to form radicals.

The hydroperoxide lyase branch of the oxylipin pathway protects against photoinhibition of photosynthesis

AbstractMain conclusionThis study describes a new role for hydroperoxide lyase branch of oxylipin biosynthesis pathway in protecting photosynthetic apparatus under high light conditions. Lipid-derived signaling molecules, oxylipins, produced by a multi-branch pathway are central in regulation of a wide range of functions. The two most known branches, allene oxide synthase (AOS) and 13-hydroperoxide lyase (HPL) pathways, are best recognized as producers of defense compounds against biotic challenges. In the present work, we examine the role of these two oxylipin branches in plant tolerance to the abiotic stress, namely excessive light. Towards this goal, we have analyzed variable chlorophyll fluorescence parameters of intact leaves of Arabidopsis thaliana genotypes with altered oxylipin profile, followed by examining the impact of exogenous application of selected oxylipins on functional activity of photosynthetic apparatus in intact leaves and isolated thylakoid membranes. Our findings unequivocally bridge the function of oxylipins to photosynthetic processes. Specifically, HPL overexpressing lines display enhanced adaptability in response to high light treatment as evidenced by lower rate constant of photosystem 2 (PS2) photoinhibition and higher rate constant of PS2 recovery after photoinhibition. In addition, exogenous application of linolenic acid, 13-hydroperoxy linolenic acid, 12-oxophytodienoic acid, and methyl jasmonate individually, suppresses photochemical activity of PS2 in intact plants and isolated thylakoid membranes, while application of HPL-branch metabolites—does not. Collectively these data implicate function of HPL branch of oxylipin biosynthesis pathway in guarding PS2 under high light conditions, potentially exerted through tight regulation of free linolenic acid and 13-hydroperoxy linolenic acid levels, as well as competition with production of metabolites by AOS-branch of the oxylipin pathway.

Trehalose protects Mn-depleted photosystem 2 preparations against the donor-side photoinhibition

Recently, it has been shown that the addition of 1M trehalose leads to the increase of the rate of oxygen photoconsumption associated with activation of electron transport in the reaction center of photosystem 2 (PS2) in Mn-depleted PS2 membranes (apo-WOC-PS2) [37]. In the present work the effect of trehalose on photoinhibition of apo-WOC-PS2 preparations (which are characterized by a high sensitivity to the donor side photoinhibition of PS2) was investigated. The degree of photoinhibition was estimated by the loss of the capability of exogenous electron donor (sodium ascorbate) to reactivate the electron transport (measured by light-induced changes of chlorophyll fluorescence yield (∆F)) in apo-WOC-PS2. It was found that 1M trehalose enhanced the Mn2+-dependent suppression of photoinhibition of apo-WOC-PS2: in the presence of trehalose the addition of 0.2μM Mn2+ (corresponding to 2 Mn2+ per one reaction center) was sufficient for an almost complete suppression of the donor side photoinhibition of the complex. In the absence of trehalose it was necessary to add 100μM Mn2+ to achieve a similar result. The effect of trehalose was observed during photoinhibition of apo-WOC-PS2 at low (15μmolphotons-1m-2) and high (200μmolphotons-1m-2) light intensity. When Mn2+ was replaced by other PS2 electron donors (ferrocyanide, DPC) as well as by Ca2+ the protective effect of trehalose was not observed. It was also found that 1M trehalose decreased photoinhibition of apo-WOC-PS2 if the samples contained endogenous manganese (1-2 Mn ions per one RC was enough for the maximum protection effect). It is concluded that structural changes in PS2 caused by the addition of trehalose enhance the capability of photochemical reaction centers of apo-WOC-PS2 to accept electrons from manganese (both exogenous and endogenous), which in turn leads to a considerable suppression of the donor side photoinhibition of PS2.

Reconstitution of water-oxidizing complex in manganese-depleted photosystem 2 preparations with synthetic manganese complexes

Four synthetic manganese complexes in which Mn atoms have different coordination environments and valence states were used to reconstitute water-oxidizing complex (WOC) in Mn-depleted photosystem 2 preparations. Three Mn-complexes restored a significant rate of electron transfer and oxygen evolution except one complex in which Mn atom ligated to the O-atoms within the ligands by covalent linkage. The effect of coordination environment of the Mn-atom within the Mn-complexes on their efficiencies in reconstituting the electron transport and oxygen evolution was analysed.

Photooxidation and photoreduction of exogenous cytochrome c by photosystem II preparations after various modifications of the water-oxidizing complex

The redox interaction of exogenous cytochrome c550 (Cyt) with PSII isolated from spinach was studied. Illumination of PSII particles in the presence of Cyt led to: (1) Cyt photooxidation by PSII reaction center (demonstrated at the first time), (2) Cyt photoreduction via O2−• photoproduced on the acceptor side of PSII, and (3) Cyt photoreduction by reduced electron carriers of PSII. A step-by-step removal of components of water-oxidizing complex was accompanied by the appearance of Cyt photooxidation, an increase in the superoxide dismutase (SOD)-dependent Cyt photoreduction (related to O2−• formation), and a decrease in the SOD-independent Cyt photoreduction. Re-addition of PsbO protein diminished the Cyt-induced restoration of electron transfer in PSII. Addition of diuron led to inhibition of these photoprocesses, while exogenous Mn2+ inhibited only the Cyt c photooxidation. The results can be important for correct measurements of O2−• photoproduction in PSII and for elucidation of the role of cytochrome c550 in cyanobacterial PSII.