[Iron-sulfur centers in the Staphylococcus aureus respiratory chain].

Using low temperature EPR spectroscopy, signals of iron-sulfur centers with g-factors of 2.02 and 1.94 were detected in the respiratory chain of St.

[Spectral properties of cytochromes from Staphylococcus aureus].

Two cytochrome b with peaks at 554 and 558 nm and cytochrome a with alpha-peak at 603 nm were found in intact cells and membranes of Staphylococcus aureus using low-temperature spectrophotometry and registration of second- and fourth-order finite difference spectra of cytochromes. Analysis of the cytochrome functioning in membranes isolated from the cells at the exponential and stationary growth phases revealed no difference in the set of these carriers. Analysis of cytochrome reduction with different substrates demonstrated identity of the cytochrome composition in the respiratory chain, reduced with NADH, lactate, alpha-glycerophosphate, malate and succinate.

[The membrane apparatus of Staphylococci in relation to acquired novobiocin resistance].

The properties of the membrane respiration apparatus of three clinical staphylococcal strains and their novobiocin resistant variants were studied comparatively. Changes in the specific activity of the respiration enzymes were shown: when the dehydrogenase activity of the membrane preparations of the sensitive and resistant variants was equal and the specific quantity of cytochromes in the novobiocin resistant staphylococci was lower, the oxidase activity of their respiration chains was increased by 60-70 per cent. Disintegration of the cells of the novobiocin resistant staphylococci resulted in a higher yield of the membrane protein, the membrane fraction being characterized by a activity of phospholipase A.

[Structure of the Micrococcus lysodeikticus respiratory chain using low concentrations of Triton X-100 and glutaric aldehyde].

Using low (0.0025 -- 0.025%) concentrations of Triton X-100, the correlation between the decrease of NADN- and malate oxidase activities and NADH- and malate dehydrogenase release in large fragments of Micrococcus lysodeikticus membranes was established.