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Title: Requirements for the phyotoactivation of the multimetric water-splitting enzyme in leaf segments following hydroxylamine induced inactivation

Thesis/Dissertation ·
OSTI ID:5806400

In weak yet optimal light intensities (30 ..mu..E.m/sup -2/.sec/sup -1/), the photoactivation of water oxidation in wheat (Triticum aestivum var. Oasis) leaf segments was obtained only after long (6-8h) dark preincubation. The complete photoactivation of O/sub 2/ evolution (..delta.. approx. 300 O/sub 2//Chl.h) required a coordinated and interdependent ligation of 4 Mn and reassembly of the 17, 23 kDa PSII polypeptides into the water oxidizing complex following initial release of these components by NH/sub 2/OH induced inactivation of the complex. Without dark preincubation, PSII was susceptible to a weak light photoinhibition process (t/sub 1/2/ approx. 2.5 min) that resulted maximally in 50% decrease in the quantum efficiency of PSII donor photooxidations and slower fluorescence rise measured in the presence of DCMU. Additional photoinhibition was not observed with either prolonged weak light illumination in the presence of translational inhibitors or 40-fold higher light intensity. However, in the absence of translational and photophosphorylation inhibitors both O/sub 2/ evolution and quantum efficiency of PSII donor photooxidations recovered from the photoinhibited state. Synthesis of two thylakoid membrane polypeptides was enhanced specifically during the light dependent recovery from the photoinhibited state. One of these polypeptides was identified as the herbicide-binding Q/sub B/ protein. Its synthesis seemed unrelated to the recovery from photoinhibition since maximal photoinhibition in the absence of protein synthesis altered neither the abundance of (/sup 35/S) labeled Q/sub B/ protein nor the (/sup 14/C) atrazine binding properties of isolated chloroplasts.

Research Organization:
Kentucky Univ., Lexington (USA)
OSTI ID:
5806400
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English