The removal of the 1-carbon of threonine can occur via threonine dehydrogenase or threonine aldolase, this carbon ending up in glycine to be liberated by the mitochondrial glycine cleavage system and producing CO(2). Alternatively, in the threonine dehydratase pathway, the 1-carbon ends up in alpha-ketobutyrate, which is oxidized in the mitochondria to CO(2). Rat hepatocytes, incubated in Krebs...

1. In the presence of the substrate benzylamine, phenethylhydrazine has been shown to be a competitive inhibitor of monoamine oxidase from rat liver and pig brain. 2. Phenethylhydrazine is also a substrate for monoamine oxidase. Reciprocal plots for hydrazine oxidation give families of intersecting lines in contrast with the parallel lines previously reported for tyramine oxidation. 3. Two poss...

The membrane-bound heterotrimeric nitrate reductase A (NarGHI) catalyzes the oxidation of quinols in the cytoplasmic membrane of Escherichia coli and reduces nitrate to nitrite in the cytoplasm. The enzyme strongly stabilizes a menasemiquinone intermediate at a quinol oxidation site (Q(D)) located in the vicinity of the distal heme b(D). Here molecular details of the interaction between the sem...

In order to characterize the structural and functional alterations in the catalytic properties of the bcl complex that are associated with specific amino acid replacements in center P cytochrome b deficient mutants, we investigated the enzymatic and myxothiazol inhibition properties of two yeast mutants (1,2), some of their revertants (3,4,5) and those of the parental strain. In the framework o...

Oxidation of ferrous iron by Thiobacillus ferrooxidans SM-4 was inhibited competitively by increasing concentrations of ferric iron or cells. A kinetic analysis showed that binding of one inhibitor did not exclude binding of the other and led to synergistic inhibition by the two inhibitors. Binding of one inhibitor, however, was affected by the other inhibitor, and the apparent inhibition const...

The occurrence of cytochrome P450 and P450-mediated pentachlorophenol oxidation in a white rot fungus Phanerochaete chrysosporium was demonstrated in this study. The carbon monoxide difference spectra indicated induction of P450 (103±13 pmol P450 per mg protein in the microsomal fraction) by pentachlorophenol. The pentachlorophenol oxidation by the microsomal P450 was NADPH-dependent at a rate ...

1. P(i) competitively inhibited succinate oxidation by intact uncoupled mitochondria in the presence of sufficient N-ethylmaleimide to block the phosphate carrier, with a K(i) of 2.5mm. 2. Of a large number of phosphate esters and phosphonate compounds, phenyl phosphate and phenylphosphonate were found to inhibit competitively uncoupled succinate oxidation by intact but not broken mitochondria....

Although a burst of oxidants has been well described with reperfusion, less is known about the oxidants generated by the highly reduced redox state and low O2 of ischemia. This study aimed to further identify the species and source of these oxidants. Cardiomyocytes were exposed to 1 h of simulated ischemia while oxidant generation was assessed by intracellular dihydroethidine (DHE) oxidation. I...

Citation: Krieger-Liszkay A and Feilke K (2016) The Dual Role of the Plastid Terminal Oxidase PTOX: Between a Protective and a Pro-oxidant Function. The plastid terminal oxidase (PTOX) is a non-heme diiron quinol oxidase that oxidizes plastoquinol and reduced O 2 to H 2 O. PTOX was discovered in the so-called immutans mutant of A. thaliana showing a variegated phenotype (Wetzel et al., 1994; Ca...

The kinetics of oxidation of ubiquinone, flavoprotein, cytochrome c, and the cytochrome b complex in skunk cabbage (Symplocarpus foetidus) mitochondria made anaerobic with succinate have been measured spectrophotometrically and fluorimetrically in the absence of respiratory inhibitor and in the presence of cyanide or antimycin A. No component identifiable by these means was oxidized rapidly eno...