Investigation of the Differences in the Local Protein Environments Surrounding Tyrosine Radicals YZ•and YD•in Photosystem II Using Wild-Type and the D2-Tyr160Phe Mutant ofSynechocystis6803†

Biochemistry ◽  
1996 ◽  
Vol 35 (5) ◽  
pp. 1475-1484 ◽  
Author(s):  
Xiao-Song Tang ◽  
Ming Zheng ◽  
Dexter A. Chisholm ◽  
G. Charles Dismukes ◽  
Bruce A. Diner
Keyword(s):  
Photosystem Ii ◽  
Wild Type ◽  
Local Protein

A Herbicide Resistant Euglena Mutant Carrying a Ser to Thr Substitution at Position 265 in the D1 Protein of Photosystem II

1992 ◽  
Vol 47 (3-4) ◽  
pp. 245-248 ◽  
Author(s):  
A. Aiach ◽  
E. Ohmann ◽  
U. Bodner ◽  
U. Johanningmeier
Keyword(s):  
Amino Acids ◽  
Sequence Analysis ◽  
Photosystem Ii ◽  
D1 Protein ◽  
Inhibitory Effect ◽  
Wild Type ◽  
Rna Sequence ◽  
Herbicide Resistant ◽  
Lower Resistance ◽  
Chlamydomonas Mutants

A herbicide resistant Euglena mutant (MSI) has been obtained by adapting wild type cells to increasing concentrations of DCMU (3-(3′,4′-dichlorophenyl)-1,1-dimethylurea). Lower resistance levels towards DCMU and metribuzin were observed in MSI when compared with Euglena or Chlamydomonas mutants with Ser 264 to Ala substitutions. RNA-sequence analysis identified a Ser to Thr change at position 265 (equivalent to position 264 in other organisms), thus making it possible to compare the influence of amino acids Ser, Ala and Thr at identical positions on the inhibitory effect of structurally different herbicides in the same species.

Photosystem II activity of wild type Synechocystis PCC 6803 and its mutants with different plastoquinone pool redox states

2016 ◽  
Vol 81 (8) ◽  
pp. 858-870
Author(s):  
O. V. Voloshina ◽  
Y. V. Bolychevtseva ◽  
F. I. Kuzminov ◽  
M. Y. Gorbunov ◽  
I. V. Elanskaya ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Wild Type ◽  
Synechocystis Pcc 6803 ◽  
Redox States ◽  
Plastoquinone Pool ◽  
Photosystem Ii Activity ◽  
Pcc 6803

scholarly journals High Field EPR Study of the Pheophytin Anion Radical in Wild Type and D1-E130 Mutants of Photosystem II inChlamydomonas reinhardtii

2001 ◽  
Vol 276 (25) ◽  
pp. 22313-22316 ◽  
Author(s):  
Pierre Dorlet ◽  
Ling Xiong ◽  
Richard T. Sayre ◽  
Sun Un
Keyword(s):  
Photosystem Ii ◽  
High Field ◽  
Anion Radical ◽  
Wild Type

scholarly journals Site-directed mutations at D1-His198 and D1-Thr179 of photosystem II in Synechocystis sp. PCC 6803: deciphering the spectral properties of the PSII reaction centre

2007 ◽  
Vol 363 (1494) ◽  
pp. 1197-1202 ◽  
Author(s):  
Eberhard Schlodder ◽  
William J Coleman ◽  
Peter J Nixon ◽  
Rachel O Cohen ◽  
Thomas Renger ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Difference Spectrum ◽  
Axial Ligand ◽  
Reaction Centre ◽  
Wild Type ◽  
Difference Spectra ◽  
Exciton Transition ◽  
Special Pair ◽  
First Approximation ◽  
Absorbance Difference

Site-directed mutations were constructed in photosystem II of Synechocystis sp. PCC6803 in which the axial ligand, D1-His198, of special pair chlorophyll P D1 was replaced with Gln and where D1-Thr179, which overlies monomeric chlorophyll Chl D1 , was replaced with His. The D1-His198Gln mutation produces a 3 nm displacement to the blue of the bleaching minimum in the Soret and in the Qy region of the – absorbance difference spectrum. To a first approximation, the bleaching can be assigned to the low-energy exciton transition of the special pair chlorophylls P D1 /P D2 . The D1-Thr179His mutation produces a 2 nm displacement to the red of the bleaching minimum in the Qy region of the ( 3 P– 1 P) absorbance difference spectrum. Analysis of the flash-induced – and ( 3 P– 1 P) absorbance difference spectra of both mutants compared with wild-type at 80 K indicate that the cation of the oxidized donor P + is predominantly localized on the chlorophyll P D1 of the special pair and that the reaction centre triplet state, produced upon charge recombination from 3 [P + Pheo − ], when the primary quinone electron acceptor Q A is doubly reduced, is primarily localized on Chl D1 .

scholarly journals Organization of the photosystem II centers and their associated antennae in the thylakoid membranes: a comparative ultrastructural, biochemical, and biophysical study of Chlamydomonas wild type and mutants lacking in photosystem II reaction centers.

1980 ◽  
Vol 87 (3) ◽  
pp. 728-735 ◽  
Author(s):  
F A Wollman ◽  
J Olive ◽  
P Bennoun ◽  
M Recouvreur
Keyword(s):  
Photosystem Ii ◽  
Fluorescence Analysis ◽  
Thylakoid Membranes ◽  
Reaction Centers ◽  
Type Number ◽  
Wild Type ◽  
Light Harvesting Complexes ◽  
Biophysical Study ◽  
In The Wild ◽  
Type C

We investigated the ultrastructure of thylakoid membranes that lacked either some or all of their Photosystem II centers in the F34SU3 and F34 mutants of Chlamydomonas reinhardtii. We obtained the following results: (a) There are no particles of the 160-A size class on the EF faces of the thylakoids in the absence of Photosystem II centers (as in F34); the F34SU3 contains 50% of the wild-type number of PSII centers and EF particles. (b) The density of the particles on the PF faces of the thylakoids is higher in the mutants than in the wild type. (c) The fluorescence analysis shows that the organization of the pigments is the same regardless of whether 50% of the PSII centers are temporarily inactivated (by preilluminating the wild type) or are actually missing from the thylakoid membrane (F34SU3). Our results, therefore, support a model in which: (a) each 160-A EF particle has only one PSII center surrounded by light-harvesting complexes and (b) part of the PSH antenna is associated with 80-A PF particles in both of the mutants and the wild type.

scholarly journals Limitations to photosynthesis by proton motive force-induced photosystem II photodamage

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Geoffry A Davis ◽  
Atsuko Kanazawa ◽  
Mark Aurel Schöttler ◽  
Kaori Kohzuma ◽  
John E Froehlich ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Proton Motive Force ◽  
Motive Force ◽  
Limiting Factor ◽  
Wild Type ◽  
Recombination Rates ◽  
Atp Production ◽  
Photosynthetic Regulation ◽  
Light Capture

The thylakoid proton motive force (pmf) generated during photosynthesis is the essential driving force for ATP production; it is also a central regulator of light capture and electron transfer. We investigated the effects of elevated pmf on photosynthesis in a library of Arabidopsis thaliana mutants with altered rates of thylakoid lumen proton efflux, leading to a range of steady-state pmf extents. We observed the expected pmf-dependent alterations in photosynthetic regulation, but also strong effects on the rate of photosystem II (PSII) photodamage. Detailed analyses indicate this effect is related to an elevated electric field (Δψ) component of the pmf, rather than lumen acidification, which in vivo increased PSII charge recombination rates, producing singlet oxygen and subsequent photodamage. The effects are seen even in wild type plants, especially under fluctuating illumination, suggesting that Δψ-induced photodamage represents a previously unrecognized limiting factor for plant productivity under dynamic environmental conditions seen in the field.

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