Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

(1) The proportion of higher plant chloroplast cytochrome b-559 oxidizable during illumination by low intensity 732 nm light increases as the pH is decreased below 6.5. At pH 5.0-5.3 total oxidation is seen and subsequent red light can cause reduction of up to 2/3 of the oxidized cytochrome. The oxidation by far red light at pH 5 is inhibited by 2 muM 2,5-dibromo-3-methyl-6-isopropyl-rho-benzoquinone whereas the red light-induced reduction is inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea. In this pH range ferricyanide-oxidized cytochrome b-559 exists in a form not reducible by ferrocyanide. (2) An increase in the amplitude of far-red induced oxidation also occurs at higher pH (up to pH 7.8) after pre-treatment of chloroplasts with substantially higher levels of light (approx. 10(6) ergs-cm-2-s-1). The degree of light activation is pH dependent, being more pronounced at lower pH. After light activation, cytochrome b-559 can be completely oxidized by far-red light in a manner reversible by red light up to pH values of 6, and the curve describing the amplitude of far-red oxidation as a function of pH is shifted by 0.5-1.0 pH unit toward higher pH. Far-red oxidation and red light reduction are again inhibited by 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone and 3-(3,4-dichlorophenyl)-1,1-dimethylurea, respectively. (3) Light activation at pH 5.2-6.0 is also manifested in a small decrease in the amplitude of subsequent dark ferrocyanide reduction, and this decrease is inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea (10 muM). (4) The effect of intramembranal acidity on the effective redox potential of cytochrome b-559 and its function is discussed.
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PMID:Stimulation of photosystem I-induced oxidation of chloroplast cytochrome b-559 by pre-illumination and by low pH. 0 40

Five substituted 2-anilinothiophenes and two substituted carbonylcyanide-phenylhydrazones were comparatively studied with respect to their capacities for inducing photooxidation of the cytochrome b-559 in chloroplast fragments and in whole cells of Chlamydomonas reinhardtii (wild type and P-700-lacking mutant Fl 5). In addition, some other compounds: antimycin A, picric acid, tetraphenylboron and NH4Cl were also tested. Cytochrome b-559 photooxidations were clearly observed in the presence of 2-(3-chloro-4-trifluoromethyl)anilino-3,5-dinitrothiophene (ANT 2p), 2-(3,4,5-trichloro)anilino-3,5-dinitrothiophene (ANT 2s), 2-(4-chloro)anilino-3,5-dinitrothiophene and, with greater amplitudes, in the presence of carbonylcyanide-p-trifluoromethoxyphenylhydrazone and carbonylcyanide-m-chlorophenylhydrazone, both in whole cells and in chloroplast fragments. Picric acid, antimycin A and tetraphenylboron were also able to induce cytochrome b-559 photooxidation in chloroplast fragments, but not in whole cells. In the wild type, the highest photoinduced redox changes were 1.1 (carbonylcyanide-p-trifluoromethoxyphenylhydrazone, carbonylcyanide-m-chlorophenyl-hydrazone) and 0.6 (ANT 2p, ANT 2s) mumol of oxidized cytochrome b-559/1 mmol of chlorophyll, corresponding to 40% and 23% of the redox changes which could be induced chemically. All these cytochrome b-559 photooxidations, the greater part of which was inhibited by 3-(3,4-dichloropheny)-1,1-dimethylurea and occurred in the mutant Fl 5, appeared to be mainly Photosystem II-dependent reactions. But 3-(3,4-dichlorophenyl)-1,1-dimethylurea-insensitive Photosystem I-dependent photooxidations of cytochrome b-559 occurred also in the wild type. On the other hand, 2-(4-dimethylamine)-anilino-3,5-dinitrothiophene, 2-N-methyl-(3-chloro-4-trifluoromethyl)anilino-3,5-dinitrothiophene and NH4Cl did not induce any cytochrome b-559 photooxidation. These results were discussed taking in consideration the nature of the molecular substitutions of the various tested substances and their respective acceleration of the deactivation reactions of the water-splitting enzyme system Y of photosynthesis capacities which had been defined elsewhere by Renger (Renger, G. (1972) Biochim. Biophys. Acta 256, 428-439) for spinach chloroplasts. Like the acceleration of the deactivation reactions of the water-splitting enzyme system Y effect, the capacity for inducing the cytochrome b-559 photooxidation appeared dependent on the acidity of the NH group and on the number of halogenous substituents in the aromatic ring of the molecule. The greatest action towards cytochrome b-559 photooxidation was obtained with the most active acceleration of the deactivation reactions of the water-splitting enzyme system Y agents: carbonylcyanide-p-trifluoromethoxyphenylhydrazone, ANT 2p and ANT 2s.
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PMID:Photooxidation of the cytochrome b-559 in the presence of various substituted 2-anilinothiophenes and of some other compounds, in Chlamydomonas reinhardtii. 50 33

1. The activity of 25 substituted 2-trifluoromethylbenzimidazoles in uncoupling oxidative phosphorylation by rat-liver mitochondria has been compared. 2. For halogen- or mixed-halogen- and alkyl-substituted analogues, uncoupling activity was proportional to the acidity of the imidazole -NH group. Tetrachloro-2-trifluoromethylbenzimidazole was the most active (50% uncoupling of oxidative phosphorylation at 7.9x10(-8)m, pK5.04). Nitro-substituted analogues were less active than predicted from pK considerations or from partition-coefficient measurements. 3. Introduction of an -NH(2) or -CO(2)H substitutent caused a loss of uncoupling activity, as did alkylation at position 1 of the imidazole ring. 4. Benzimidazoles active as uncouplers stimulated mitochondrial adenosine triphosphatase but not all stimulated the oxidation of succinate in the absence of a phosphate acceptor. 5. 4,5-Dichloro-2-trifluoromethylbenzimidazole inhibited the succinate-oxidase system at about the same concentration required for uncoupling (0.52mum for 50% inhibition of both activities) and the site of this inhibition appears to lie between succinate dehydrogenase and cytochrome b.
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PMID:Properties of substituted 2-trifluoromethylbenzimidazoles as uncouplers of oxidative phosphorylation. 429 94

A series of antimycin A analogues was synthesized by modifying the salicylic acid moiety, whereas the portion of the molecule corresponding to the natural dilactone-ring moiety was fixed as di-n-octyl L-glutamate. To probe the structure of the antimycin A binding site, the structural factors of the salicylic acid moiety required for inhibitory action were examined by means of structure-activity studies with intact rat-liver mitochondria and the cytochrome bc1 complex isolated from bovine heart mitochondria. As suggested earlier (Rieske, J.S. (1976) Biochim. Biophys. Acta 456, 195-247), the phenolic OH was very important for inhibition. For the derivatives which do not possess a formylamino group in the 3-position (ortho to the phenolic OH), the inhibitory activity tended to increase as the electron-withdrawing property of the substituent increased, i.e., as the acidity of the phenolic OH group increased. This indicates that the acidity of the phenolic OH is an important factor governing inhibition. While the electron-withdrawing property of the formylamino group itself is rather poor, 3-formylamino derivatives elicited potent activity. The conformation of the 3-formylamino group was also found to be a very important factor in establishing inhibitory activity. In addition, the bulkier the moiety corresponding to the 3-formylamino group, the lower the activity. These results demonstrate that the presence of the 3-formylamino group, and its proper conformation, are needed for a close fitting of antimycin A to its binding domain. Although the inhibitors that lack a 3-formylamino group retained fairly potent activity, their effects on the reduction of cytochromes b and c1 were somewhat different from those of natural antimycin A, indicating that the 3-formylamino group is essential for inhibitor binding to the cytochrome bc1 complex in the same manner as natural antimycin A. It is concluded that both the 3-formylamino group and the phenolic OH of antimycin A make important contributions to specific interactions with the amino acid residues of the cytochrome b.
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PMID:Structural factors of antimycin A molecule required for inhibitory action. 818 Feb 32