Assignment of the QyAbsorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers†

Biochemistry ◽  
2000 ◽  
Vol 39 (47) ◽  
pp. 14583-14594 ◽  
Author(s):  
David H. Stewart ◽  
Peter J. Nixon ◽  
Bruce A. Diner ◽  
Gary W. Brudvig
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Optical Spectroscopy ◽  
Reaction Centers ◽  
Wild Type

Pigment Organization and Their Interactions in Reaction Centers of Photosystem II:  Optical Spectroscopy at 6 K of Reaction Centers with Modified Pheophytin Composition†

Biochemistry ◽  
2001 ◽  
Vol 40 (38) ◽  
pp. 11472-11482 ◽  
Author(s):  
Marta Germano ◽  
Anatoli Ya. Shkuropatov ◽  
Hjalmar Permentier ◽  
Rik de Wijn ◽  
Arnold J. Hoff ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Optical Spectroscopy ◽  
Reaction Centers

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.

Low-temperature (77 K) phosphorescence of triplet chlorophyll in isolated reaction centers of photosystem II

2015 ◽  
Vol 125 (1-2) ◽  
pp. 43-49 ◽  
Author(s):  
Konstantin V. Neverov ◽  
Alexander A. Krasnovsky ◽  
Alexey A. Zabelin ◽  
Vladimir A. Shuvalov ◽  
Anatoly Ya. Shkuropatov
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Reaction Centers

scholarly journals D1 protein variants in Photosystem II from Thermosynechococcus elongatus studied by low temperature optical spectroscopy

2010 ◽  
Vol 1797 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Joseph L. Hughes ◽  
Nicholas Cox ◽  
A. William Rutherford ◽  
Elmars Krausz ◽  
Thanh-Lan Lai ◽  
...  
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Optical Spectroscopy ◽  
D1 Protein ◽  
Protein Variants

Fluorescence and Photochemical Properties of Plants with Defective Photosystem II

1980 ◽  
Vol 35 (5-6) ◽  
pp. 461-466 ◽  
Author(s):  
Wilhelm Menke ◽  
Georg H. Schmid
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Emission Spectrum ◽  
Photosystem I ◽  
Room Temperature ◽  
Fluorescence Emission ◽  
Fluorescence Emission Spectrum ◽  
Wild Type ◽  
Fully Functioning ◽  
Fluorescence Energy

Abstract The mykotrophic orchid Neottia nidus-avis does not evolve oxygen in the light but is able to perform photophosphorylation. The low temperature fluorescence emission spectrum lacks the 680 and 690 nm bands. Hence, the spectroscopic chlorophyll a forms which are attributed to photosystem II do not occur in plastids of this orchid. The low temperature excitation spectrum of photosystem I fluorescence exhibits a maximum at 666 nm. The position of this maximum appears not to be influenced by energy transfer and corresponds to the absorption maximum of the chlorophyll form which emits the photosystem I fluorescence. Energy migration, however, occurs from carotenoids whose absorption spectrum is shifted to longer wavelengths and which cause the yellow-brown color of the Neottia plastids. Room temperature fluorescence emission shows after the onset of light no variable part. Despite the fact that plastids of the tobacco mutant NC 95 at most evolve only traces of oxygen the low temperature emission spectrum shows the three bands which are usually observed with fully functioning chloroplasts. However, the two bands at 680 and 690 nm are distinctly lower than with the wild type. The variable portion of room temperature fluorescence is barely detectable. In line with the very low capacity for oxygen evolution, rates of electron transport partial reactions in the region of photosystem II are extremely low. In agreement with this observation no 690 nm absorption change signal is detected. However, a normal P+700 signal is seen. In the presence of electron donors like reduced phenazine methosulfate the decay time of the P+700 signal is faster than with the wild type. The yellow tobacco mutant Su/su var. aurea which exhibits at high light intensities higher rates of photosynthesis than the wild type shows at low temperature an emission spectrum with stronger photosystem II bands than the wild type.

Fluorescence Decay Kinetics of Wild Type and D2-H117N Mutant Photosystem II Reaction Centers Isolated fromChlamydomonas reinhardtii

2000 ◽  
Vol 104 (19) ◽  
pp. 4777-4781 ◽  
Author(s):  
Heather G. Johnston ◽  
Jun Wang ◽  
Stuart V. Ruffle ◽  
Richard T. Sayre ◽  
Terry L. Gustafson
Keyword(s):  
Photosystem Ii ◽  
Fluorescence Decay ◽  
Reaction Centers ◽  
Wild Type ◽  
Decay Kinetics ◽  
Fluorescence Decay Kinetics ◽  
Kinetics Of
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