A new type of mitochondrial encephalomyopathy with stroke-like episodes due to cytochrome oxidase deficiency.
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Partial DNA and amino acid sequences translated from the mitochondrial cytochrome subunit I gene (408 bp) of 17 mite species have been used for analyzing the phylogenetic relationships within the terrestrial Parasitengona (Trombidia). Due to mutational saturation of the third codon position, only first and second codon positions and amino acid sequences were analyzed, applying neighbor-joining, maximum-parsimony, and maximum-likelihood tree-building methods. The reconstructed trees revealed similar topologies of taxa; however, the phylogenetic relationships could be convincingly resolved only within several trombidioid taxa. The proposed basic relationships within the Parasitengona, in particular those of Calyptostomatoidea, Smarididae, and Erythraeidae, were poorly supported in bootstrap tests. A comparison of the presented gene tree with a phylogenetic tree based upon traditional characters revealed only few contradictions in nodes only weakly supported by morphological data. The most astonishing result is the proposed early derivative position of Microtrombidiidae within the terrestrial Parasitengona.
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The intravenous administration of acetazolamide to rats caused a prompt oxidation of cytochrome a,a3 that was associated with an increase in the rate at which this cytochrome underwent additional oxidation and reductive recovery after electrical stimulation of the cerebral cortex. These effects were not observed in animals made hypercapnic after ventilation with 5% CO2. The speed with which these and other metabolic and physiological events occur, after administering the drug, suggests that acetazolamide exerts its effects by complex mechanisms and that the site of action may be in the region of the blood-brain barrier, an area rich in carbonic anhydrase, and noradrenergic innervation.
In an effort to determine the steady-state redox properties of Pseudomonas aeruginosa cytochrome cd1, changes in absorption spectra after the addition of excess reductant (ascorbate, ferrous ethylenediaminetetraacetic acid) were monitored for degassed unliganded enzyme and samples in the presence of CO and CN- at pH 6.0, 8.0, or 10.0. Plots of [c2+]/[c3+] vs. [d2+]/[d3+] indicate that a "pseudoequilibrium" was reached for all samples at pH 8.0. Calculated values of delta Ed-c, the difference in reduction potential between the heme c and heme d moieties, at pH 8.0 were -25 +/- 5 (unliganded), -10 +/- 5 (enzyme-CO), and -25 +/- 5 mV (enzyme-CN). Relative rates of heme c and heme d reduction were found to be dependent upon type of ligand, reductant, and pH. Evidence for a cooperative heme c-heme d interaction is discussed.
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