期刊
CELLS
卷 11, 期 17, 页码 -出版社
MDPI
DOI: 10.3390/cells11172680
关键词
photosynthetic inhibitors; copper; metalorganic complexes; photosystem II; oxygen evolution; aromatic amino acids intrinsic fluorescence
类别
资金
- Russian Science Foundation [19-14-00118]
- AzSF [E.IF-GAT-6-2021-2(39)-13/06/3-M-06]
- Ministry of Science and Higher Education of the Russian Federation [122050400128-1]
- Distinguished Scientists Fellowship Program, King Saud University, Saudi Arabia
The effects of the [CuL2]Br-2 complex on PSII activity and chlorophyll fluorescence yield in spinach were investigated. The complex was found to inhibit photosynthetic oxygen evolution and the photoreduction of the primary quinone electron acceptor. The inhibition depended on the concentration of [CuL2]Br-2 and was not affected by artificial electron donors.
The effects of the novel [CuL2]Br-2 complex (L = bis{4H-1,3,5-triazino [2,1-b]benzothiazole-2-amine,4-(2-imidazole)}copper(II) bromide complex) on the photosystem II (PSII) activity of PSII membranes isolated from spinach were studied. The absence of photosynthetic oxygen evolution by PSII membranes without artificial electron acceptors, but in the presence of [CuL2]Br-2, has shown that it is not able to act as a PSII electron acceptor. In the presence of artificial electron acceptors, [CuL2]Br-2 inhibits photosynthetic oxygen evolution. [CuL2]Br-2 also suppresses the photoinduced changes of the PSII chlorophyll fluorescence yield (F-V) related to the photoreduction of the primary quinone electron acceptor, Q(A). The inhibition of both characteristic PSII reactions depends on [CuL2]Br-2 concentration. At all studied concentrations of [CuL2]Br-2, the decrease in the F-M level occurs exclusively due to a decrease in Fv. [CuL2]Br-2 causes neither changes in the F-0 level nor the retardation of the photoinduced rise in F-M, which characterizes the efficiency of the electron supply from the donor-side components to Q(A) through the PSII reaction center (RC). Artificial electron donors (sodium ascorbate, DPC, Mn2+) do not cancel the inhibitory effect of [CuL2]Br-2. The dependences of the inhibitory efficiency of the studied reactions of PSII on [CuL2]Br-2 complex concentration practically coincide. The inhibition constant Ki is about 16 mu M, and logKi is 4.8. As [CuL2]Br-2 does not change the aromatic amino acids' intrinsic fluorescence of the PSII protein components, it can be proposed that [CuL2]Br-2 has no significant effect on the native state of PSII proteins. The results obtained in the present study are compared to the literature data concerning the inhibitory effects of PSII Cu(II) aqua ions and Cu(II)-organic complexes.
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