[N-hydroxylation of sulfanilamide to p-hydroxylaminobenzolsulfonamide by liver microsomes].
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Biomedical subjects
Publications and source records attributed to R K Thauer.
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Carbon monoxide dehydrogenase of anaerobic bacteria catalyzes the reversible conversion of CO to "CO2". With the enzyme from Peptostreptococcus productus it is shown that CO2 rather than HCO3- (H2CO3) is the active species of "CO2" formed by this dehydrogenase.
Strictly anaerobic microorganisms relating to various physiological groups were screened for catalase and superoxide dismutase (SOD) activity. All of the investigated anaerobes possessed the SOD activity, necessary for protection against toxic products of oxygen reduction. High specific activities of SOD were found in Acetobacterium woodii and Acetobacterium wieringae. Most of the investigated clostridia and acetogens were catalase-negative. A significant activity of catalase was found in Thermohydrogenium kirishiense, in representatives of the genus Desulfotomaculum, and in several methanogens. Methanobrevibacter arboriphilus had an exceptionally high catalase activity after growth in medium supplemented with hemin. Hemin also produced a strong positive effect on the catalase activity in many other anaerobic microorganisms. In methanogens, the activities of the enzymes of antioxidant defense varied in wide ranges depending on the stage of growth and the energy source.