Structure, Electron Transfer Chain of Photosystem II and the Mechanism of Water Splitting

2021 ◽  
pp. 3-38
Author(s):  
Jian-Ren Shen ◽  
Yoshiki Nakajima ◽  
Fusamichi Akita ◽  
Michihiro Suga
1983 ◽  
Vol 38 (9-10) ◽  
pp. 793-798 ◽  
Author(s):  
W. S. Cohen ◽  
J. R. Barton

Photosystem II particles that retain the ability to evolve O2 have been used to examine acceptor and inhibitor sites in the photosynthetic electron transfer chain between Q and plastoquinone. Employing the water to dichlorobenzoquinone reaction to assay photosystem II activity, we have demonstrated that electron transport in thylakoids and particles is equally sensitive to inhibition by DCMU. dinoseb, metribuzin, HQNO and DBMIB. Based on differential sensitivity to inhibition by DCMU vs. HQNO or DBMIB, we suggest that when synthetic quinones, e.g. 2,6-dichlorobenzoquinone operate as Hill reagents in particles they are reduced primarily by the plastoquinone pool. When synthetic quinones, e.g. 5,6-methylenedioxy-2,3-dimethyl benzoquinone act as autoxidizable acceptors they accept electron from the Q/B complex at a point that is located between the DCMU and HQNO (DBMIB) inhibition sites.


2012 ◽  
Vol 109 (39) ◽  
pp. 15578-15583 ◽  
Author(s):  
J. D. Megiatto ◽  
A. Antoniuk-Pablant ◽  
B. D. Sherman ◽  
G. Kodis ◽  
M. Gervaldo ◽  
...  

2016 ◽  
Vol 83 (3) ◽  
Author(s):  
Xin Zhang ◽  
Fei Ma ◽  
Xi Zhu ◽  
Junying Zhu ◽  
Junfeng Rong ◽  
...  

ABSTRACT Nitrite, a common form of inorganic nitrogen (N), can be used as a nitrogen source through N assimilation. However, high levels of nitrite depress photosynthesis in various organisms. In this study, we investigated which components of the photosynthetic electron transfer chain are targeted by nitrite stress in Synechocystis sp. strain PCC 6803 cells. Measurements of whole-chain and photosystem II (PSII)-mediated electron transport activities revealed that high levels of nitrite primarily impair electron flow in PSII. Changes in PSII activity in response to nitrite stress occurred in two distinct phases. During the first phase, which occurred in the first 3 h of nitrite treatment, electron transfer from the primary quinone acceptor (QA) to the secondary quinone acceptor (QB) was retarded, as indicated by chlorophyll (Chl) a fluorescence induction, S-state distribution, and QA − reoxidation tests. In the second phase, which occurred after 6 h of nitrite exposure, the reaction center was inactivated and the donor side of photosystem II was inhibited, as revealed by changes in Chl fluorescence parameters and thermoluminescence and by immunoblot analysis. Our data suggest that nitrite stress is highly damaging to PSII and disrupts PSII activity by a stepwise mechanism in which the acceptor side is the initial target. IMPORTANCE In our previous studies, an alga-based technology was proposed to fix the large amounts of nitrite that are released from NOX-rich flue gases and proved to be a promising industrial strategy for flue gas NOX bioremediation (W. Chen et al., Environ Sci Technol 50:1620–1627, 2016, https://doi.org/10.1021/acs.est.5b04696 ; X. Zhang et al., Environ Sci Technol 48:10497–10504, 2014, https://doi.org/10.1021/es5013824 ). However, the toxic effects of high concentrations of nitrite on algal cells remain obscure. The analysis of growth rates, photochemistry, and protein profiles in our study provides important evidence that the inhibition by nitrite occurs in two phases: in the first phase, electron transfer between QA − and QB is retarded, whereas in the second, the donor side of PSII is affected. This is an excellent example of investigating the “early” inhibitory effects (i.e., within the first 6 h) on the PSII electron transfer chain in vivo. This paper provides novel insights into the mechanisms of nitrite inhibition of photosynthesis in an oxygenic phototrophic cyanobacterium.


2009 ◽  
Vol 75 (12) ◽  
pp. 4202-4205 ◽  
Author(s):  
Wei Wang ◽  
Feng-Qing Wang ◽  
Dong-Zhi Wei

ABSTRACT A new cytochrome P450 monooxygenase, FcpC, from Streptomyces virginiae IBL-14 has been identified. This enzyme is found to be responsible for the bioconversion of a pyrano-spiro steroid (diosgenone) to a rare nuatigenin-type spiro steroid (isonuatigenone), which is a novel C-25-hydroxylated diosgenone derivative. A whole-cell P450 system was developed for the production of isonuatigenone via the expression of the complete three-component electron transfer chain in an Escherichia coli strain.


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