Succinate oxidase activity in the absence of ubiquinone

FEBS Letters ◽  
1971 ◽  
Vol 13 (5) ◽  
pp. 265-266 ◽  
Author(s):  
S.P.J. Albracht ◽  
H. Van Heerikhuizen ◽  
E.C. Slater
1980 ◽  
Vol 45 (2) ◽  
pp. 641-652
Author(s):  
Petr Zbořil

Semiquinone is an intermediary product of the oxidation of daphnetin (7,8-dihydroxycoumarin) and esculetin (6,7-dihydroxycoumarin) by diphenol oxidase; its concentration rapidly decreases. When the oxidation is effected by ferricytochrome c, the concentration of the semiquinone remains practically constant for a long period. Similarly, the ability of the products of daphnetin oxidation by diphenol oxidase to inhibit succinate oxidase activity in mitochondrial fragments rapidly decreases with time; the decrease is considerably slower in the case of cytochrome c. The inhibitory activity of the product decreases with time also during esculetin oxidation by ferricyanide. This indicates that the inhibitory effects must be ascribed predominantly to the semiquinone, the quinone is less efficient. The inhibition of succinate oxidase or succinate dehydrogenase was strongly decreased when the enzyme preparation of Keilin and Hartree was incubated with esculetin and ferricyanide in the presence of KCN or under anaerobic conditions. This demonstrates that the reaction of the inhibitor with the enzyme either involves subsequent oxidations or that the inhibitor preferentially reacts with the oxidized form of the sensitive component of the respiratory chain. The second alternative is very little probable since there is no correlation between the degree of inhibition and the binding of the inhibitor to mitochondrial fragments.


1980 ◽  
Vol 188 (1) ◽  
pp. 141-144 ◽  
Author(s):  
J Vanderleyden ◽  
C Peeters ◽  
H Verachtert ◽  
H Bertrand

The alternative-oxidase-mediated succinate oxidase activity of Neurospora crassa decreases drastically when mitochondria are fractionated into submitochondrial particles or treated with deoxycholate. The activity, however, can be completely restored in the presence of nucleoside 5′-monophosphates. The purine nucleoside 5′-monophosphates are more effective than the pyrimidine homologues. 5′-GMP gives a 10-fold stimulation of the alternative-oxidase-mediated succinate oxidase activity in submitochondrial particles. A comparison is made with the results obtained earlier with Moniliella tomentosa [Hanssens & Verachtert (1976) J. Bacteriol. 125, 825–835; Vanderleyden, Van Den Eynde & Verachtert (1980) Biochem. J. 186, 309–316].


2006 ◽  
Vol 281 (16) ◽  
pp. 11357-11365 ◽  
Author(s):  
Elena Maklashina ◽  
Tina M. Iverson ◽  
Yelizaveta Sher ◽  
Violetta Kotlyar ◽  
Juni Andréll ◽  
...  

1975 ◽  
Vol 21 (3) ◽  
pp. 343-352 ◽  
Author(s):  
D. A. Farago ◽  
L. N. Gibbins

Chemostat cultures of Erwinia amylovora 595, grown in mineral salts – nicotinic acid medium at 30 °C, and limited by D-glucose concentrations in the presence of dissolved oxygen tensions (D.O.T.) greater than about 6 mm Hg, became limited by oxygen availability below about 4 mm Hg. This latter limitation was accompanied by a marked increase in acid production as the D.O.T. was depressed. The transition between D-glucose- and oxygen-limitation was also characterized by a maximum in succinate oxidase activity, and a minimum in the in situ respiration. D-Glyceraldehyde-3-phosphate dehydrogenase and D-fructose-1,6-diphosphate aldolase showed small reductions in specific activity in the region 4–6 mm Hg D.O.T., but further reduction to 2 mm Hg resulted in a marked increase in the specific activity of aldolase. Malate dehydrogenase followed the converse trend, and attained very low activity levels when the D.O.T. decreased beyond the lower limits of detection. The in situ respiration was maximal at 2 mm Hg D.O.T., while potential respiration values were minimal at 2 mm Hg, and maximal at about 8 mm Hg D.O.T. The in situ respiration rate was proportional to dilution rate (D), in presence of excess oxygen, up to 0.18 h−1, after which a marked diminution occurred and continued until the wash-out rate was attained. Succinate oxidase activity decreased with increase in dilution rate, but remained constant above D = 0.18 h−1. Malate dehydrogenase showed a persistent decline with increase in dilution rate, while D-glyceraldehyde-3-phosphate activity increased somewhat at higher dilution rates. The data are interpreted in terms of two transition points, at 6 and 2 mm Hg D.O.T., and of a change from respiratory to fermentative metabolism at low D.O.T., and at high dilution rates.


1984 ◽  
Vol 224 (3) ◽  
pp. 955-960 ◽  
Author(s):  
P Saikumar ◽  
C K R Kurup

Administration of 2-methyl-4-dimethylaminobenzene in the diet (0.1%, w/w) for 85-90 days doubled the content of mitochondria in the livers of rats. The azodye was covalently bound to liver proteins, and about 15% of the amount found in liver was associated with the mitochondrial fraction. Mitochondria isolated from the livers of azodye-fed animals showed drastically lowered ability to oxidize NAD+-linked substrates. The inhibited electron-transfer step was the reduction of ubiquinone. The organelles showed a large increase in succinate oxidase activity. The activity of cytochrome oxidase and the content of cytochrome aa3 were substantially higher in these organelles. Azodye-fed animals showed depressed serum cholesterol concentrations. The content of ubiquinone in liver also registered a small increase.


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