Journal Article

Differential Effects of Urea/Triazine-type and Phenol-type Photosystem II Inhibitors on Inactivation of the Electron Transport and Degradation of the D1 Protein during Photoinhibition

Yoshihiro Nakajima, Shigeo Yoshida and Taka-aki Ono

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 37, issue 5, pages 673-680
Published in print July 1996 | ISSN: 0032-0781
e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a028997
Differential Effects of Urea/Triazine-type and Phenol-type Photosystem II Inhibitors on Inactivation of the Electron Transport and Degradation of the D1 Protein during Photoinhibition

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The loss of PSII activity (water → silicomolybdate) and the degradation of the D1 protein during photoinhibitory illumination were studied in the presence of the various PSII inhibitors that bind to the QB-site to interrupt the electron transfer from QA to QB, and the following results were obtained, (i) The inactivation of PSII was suppressed in the presence of urea/triazine-type inhibitors but was enhanced in the presence of phenol-type inhibitors, (ii) The urea/triazine-type inhibitors retarded not only the degradation of the D1 protein but also the formation of the 41 kDa adduct of the Dl protein and the α-subunit of Cyt bm. (iii) The phenol-type inhibitors did not affect the degradation of the D1 protein but enhanced the formation of the 41 kDa adduct. (iv) The 23 and 9 kDa fragments of the D1 protein, induced by dark incubation with PNO8, were further degraded by photoinhibitory illumination, (v) Photoinactivation of PSII was not suppressed by DCMU, a urea/triazine-type inhibitor, after the QB-site had been modified by trypsin. These and other results are discussed with respect to the possibility of a conformational change at the QB-site of the Dl protein, induced by the binding of a PSII inhibitor, and the effects of such a change on the processes of photoinhibition.

Keywords: D1 protein; Herbicides; Photoinhibition; Photosystem II; QA; QB

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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