Inhibition of photosystem II electron transport and structure-activity relationships among herbicidally active 3-butenanilides

1992 ◽  
Vol 43 (2) ◽  
pp. 162-170 ◽  
Author(s):  
R.J. Eilers ◽  
G.D. Crouse ◽  
G.L. Durst ◽  
C.J. Manly ◽  
J.D. Webster ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Structure Activity Relationships ◽  
Structure Activity

Photosystem II Inhibition by Pyran-enamine Derivatives

1993 ◽  
Vol 48 (3-4) ◽  
pp. 163-167
Author(s):  
Koichi Yoneyama ◽  
Yoshihiro Nakajima ◽  
Masaru Ogasawara ◽  
Hitoshi Kuramochi ◽  
Makoto Konnai ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Thylakoid Membranes ◽  
Major Determinant ◽  
Ps Ii ◽  
Structure Activity Relationships ◽  
Structure Activity

Abstract Through the studies on structure-activity relationships of 5-acyl-3-(1-aminoalkylidene)-4-hydroxy-2 H-pyran-2,6(3 H)-dione derivatives in photosystem II (PS II) inhibition, overall lipophilicity of the molecule was found to be a major determinant for the activity. In the substituted N -benzyl derivatives, not only the lipophilicity but also the electronic and steric characters of the substituents greatly affected the activity. Their mode of PS II inhibition seemed to be similar to that of DCMU , whereas pyran-enamine derivatives needed to be highly lipophilic to block the electron transport in thylakoid membranes, which in turn diminished the permeability through biomembranes.

scholarly journals Synthesis and Antimycobacterial and Photosynthesis-Inhibiting Evaluation of 2-[(E)-2-Substituted-ethenyl]-1,3-benzoxazoles

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Ales Imramovsky ◽  
Jan Kozic ◽  
Matus Pesko ◽  
Jirina Stolarikova ◽  
Jarmila Vinsova ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Inhibitory Action ◽  
Spinacia Oleracea ◽  
Photosynthetic Electron Transport ◽  
Inhibiting Activity ◽  
Donor Side ◽  
Structure Activity Relationships ◽  
Structure Activity

A series of twelve 2-[(E)-2-substituted-ethenyl]-1,3-benzoxazoles was designed. All the synthesized compounds were tested against three mycobacterial strains. The compounds were also evaluated for their ability to inhibit photosynthetic electron transport (PET) in spinach (Spinacia oleraceaL.) chloroplasts. 2-[(E)-2-(4-Methoxyphenyl)ethenyl]-1,3-benzoxazole, 2-[(E)-2-(2,3-dihydro-1-benzofuran-5-yl)ethenyl]-1,3-benzoxazole and 2-{(E)-2-[4-(methylsulfanyl)phenyl]ethenyl}-1,3-benzoxazole showed the highest activity againstM. tuberculosis,M. kansasii,andM. avium, and they demonstrated significantly higher activity againstM. aviumandM. kansasiithan isoniazid. The PET-inhibiting activity of the most activeortho-substituted compound 2-[(E)-2-(2-methoxyphenyl)ethenyl]-1,3-benzoxazole was IC50= 76.3 μmol/L, while the PET-inhibiting activity ofpara-substituted compounds was significantly lower. The site of inhibitory action of tested compounds is situated on the donor side of photosystem II. The structure-activity relationships are discussed.

Phloroglucinol Derivatives as Potent Photosystem II Inhibitors

1990 ◽  
Vol 45 (5) ◽  
pp. 317-321 ◽  
Author(s):  
Koichi Yoneyama ◽  
Makoto Konnai ◽  
Ichiro Honda ◽  
Shigeo Yoshida ◽  
Nobutaka Takahashi ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Eucalyptus Grandis ◽  
Binding Domain ◽  
Side Chains ◽  
Ps Ii ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Phloroglucinol Derivatives ◽  
New Type

Studies on structure/activity relationships of phloroglucinol derivatives that had been designed based on the structures of grandinol and homograndinol. potent photosystem II (PS II) inhibitors in Eucalyptus grandis, revealed that two electron-withdrawing groups which differ by their electron-withdrawing power on a phloroglucinol nucleus were essential for activity. A larger difference in the electron-withdrawing power between the two groups enhanced the activity, and 3-nitro-phloroglucinecarboxamides and the corresponding thioamides were the most active ones when they had proper lipophilic side chains. Their binding domain seems to overlap with those of DCMU and atrazine, whereas they may approach to the site in a similar manner to that of phenol type inhibitors. Accordingly, the phloroglucinol derivatives represent a new type of PS II inhibitors.

Quantitative structure-activity relationships in the inhibition of photosystem II in chloroplasts by phenylureas

1984 ◽  
Vol 32 (1) ◽  
pp. 133-144 ◽  
Author(s):  
Emil Kakkis ◽  
Vincent C. Palmire ◽  
Cynthia D. Strong ◽  
Walter Bertsch ◽  
Corwin Hansch ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Quantitative Structure ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Quantitative Structure Activity Relationships

scholarly journals Structure–Activity Relationships of Hierarchical Three-Dimensional Electrodes with Photosystem II for Semiartificial Photosynthesis

Nano Letters ◽  
2019 ◽  
Vol 19 (3) ◽  
pp. 1844-1850 ◽  
Author(s):  
Xin Fang ◽  
Katarzyna P. Sokol ◽  
Nina Heidary ◽  
Tarek A. Kandiel ◽  
Jenny Z. Zhang ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Three Dimensional ◽  
Structure Activity Relationships ◽  
Structure Activity

Structure-Activity Relationships and Physiological Aspects of New Photosynthetic Electron Transport Inhibitors, 3-Alkylaminoalkyliden-2H-pyran-2,4(3H)-diones (APs)

1988 ◽  
Vol 43 (11-12) ◽  
pp. 857-861 ◽  
Author(s):  
Tadao Asami ◽  
Hiroyuki Koike ◽  
Yorinao Inoue ◽  
Nobutaka Takahashi ◽  
Shigeo Yoshida
Keyword(s):  
Electron Transport ◽  
Photosynthetic Electron Transport ◽  
Structural Requirement ◽  
Structure Activity Relationships ◽  
New Class ◽  
Structure Activity ◽  
Transport Inhibition ◽  
Transport Inhibitors

3-Aminoalkylidene-2H-pyran-2,4(3H)-diones (APs), possessing a conjugated enamino moiety which is common to cyanoacrylates and 2-aminoalkylidenecyclohexane-1,3-diones (ACs), were found as a new class of photosynthetic electron transport inhibitors. Although the structural requirement of APs for photosynthetic electron transport inhibition was very similar to that of cyanoacrylates and ACs, thermoluminescence measurements indicated that the binding manner of APs to D 1 protein was totally different from that of other inhibitors.

Sign in / Sign up

Export Citation Format

Share Document