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Obligate anaerobic organisms

The anaerobic mode of protein utilization is entirely possible in theory and in practice. Oxygen is not required for protein and nitrogen catabolism until the final stages of amino acid deamination have been reached. Complete anaerobic catabolism of proteins and nitrogen compounds (to the point where the final products C02, HjO and NH3 appear) has been known for a long time in prokaryotic organisms, but in eukaryotes only in parasitic worms, which are obligate anaerobes (von Brand, 1946). However, in recent decades, anaerobic metabolism of proteins has been found in some aquatic... [Pg.35]

Microbes capable of carrying out fermentations are classified as either facultative or obligate anaerobes. Facultative anaerobes, such as the enterobacteria, utilize 02 if and when it is present, but if it is absent, they carry out fermentative metabolism. In contrast, obligate anaerobes are unable to synthesize the components of electron transport systems consequently, they cannot grow as aerobes. Moreover, many of the obligate anaerobes cannot even tolerate oxygen and perish in air these organisms are referred to as strict anaerobes. [Pg.105]

Table I also shows the great diversity of organisms in which iron—sulfur proteins have been detected. Thus far there is no organism which when appropriately examined has not contained an iron-sulfur protein, either in the soluble or membrane-bound form. Iron-sulfur proteins catalyze reactions of physiological importance in obligate anaerobic bacteria, such as hydrogen uptake and evolution, ATP formation, pyruvate metabolism, nitrogen fixation, and photosynthetic electron transport. These properties and reactions can be considered primitive and thus make iron-sulfur proteins a good place to start the study of evolution. These key reactions are also important in higher organisms. Other reactions catalyzed by iron-sulfur proteins can be added such as hydroxylation, nitrate and nitrite reduction, sulfite reduction, NADH oxidation, xanthine oxidation, and many other reactions (Table II). Table I also shows the great diversity of organisms in which iron—sulfur proteins have been detected. Thus far there is no organism which when appropriately examined has not contained an iron-sulfur protein, either in the soluble or membrane-bound form. Iron-sulfur proteins catalyze reactions of physiological importance in obligate anaerobic bacteria, such as hydrogen uptake and evolution, ATP formation, pyruvate metabolism, nitrogen fixation, and photosynthetic electron transport. These properties and reactions can be considered primitive and thus make iron-sulfur proteins a good place to start the study of evolution. These key reactions are also important in higher organisms. Other reactions catalyzed by iron-sulfur proteins can be added such as hydroxylation, nitrate and nitrite reduction, sulfite reduction, NADH oxidation, xanthine oxidation, and many other reactions (Table II).

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See also in sourсe #XX -- [ Pg.141 , Pg.157 ]




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