The preparation of Dl/D2/cytochrome 6559 complex isolated from pea (Pisum sativum h.) was photoinactivated by "white light" (140 W m‘2) at 20 and 4 "C in both the presence and absence of oxygen. The inactivation was followed by measuring the decline of the photoinduced absorbance change A/4683 (the photoaccumulation of reduced pheophytin), by measuring absorption spectra and fluorescence emission, and by polypeptide analysis. In the presence of oxygen, the ability of the DUDUcyi 6559 complex to acciunulate reduced pheophytin was lost with the halftime im of about 3 min and fluorescence quantum yield declined with ti/2 of about 30 min at both 20 and 4 ^C. The D\ and Dl polypeptides were rapidly modified at 20 °C as reflected by the presence of their large aggregates at the start of the electrophoretic gel and by a decrease of the mobility of remaining Dl and Dl monomers. This modification was substantially limited at 4 “C. Subímits of cytochrome 6559 were not modified at any temperature. When oxygen was removed, the halftime of the A/1683 decline increased by about one order of magnitude, fluorescence emission did not decline, but slightly increased, and the polypeptide pattem was only slightly affected during irradiation.
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., A. A. Khorobrykh, D. V. Yanykin, V. V. Klimov., and Obsahuje bibliografické odkazy
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. and G. Y. Chen ... [et al.].