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Cytochromes c ‐dependent aerobic respiration of Paracoccus denitrificans
Author(s) -
Kaplan Petr,
Kučera Igor
Publication year - 1993
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620330606
Subject(s) - paracoccus denitrificans , periplasmic space , cytochrome , cyanide , cytochrome c oxidase , cytochrome c , biochemistry , chemistry , respiratory chain , oxygen , coenzyme q – cytochrome c reductase , oxidase test , electron transport chain , enzyme , inorganic chemistry , organic chemistry , mitochondrion , escherichia coli , gene
Terminal parts of the respiratory chain of Paracoccus denitrificans containing cytochromes c have been investigated through the use of NNN′Nprime;‐tetramethyl‐p‐phenylenediamine (TMPD) as an electron donor. The cells have been shown to possess two major membrane bound TMPD oxidases characterized by their different sensitivities to cyanide. The more sensitive one, identified as cytochrome aa 3 , appears to be produced under oxygen‐rich growth conditions, whereas a less sensitive and as yet uncharacterized enzyme accompanied with only moderate amounts of cytochrome aa 3 functions when oxygen becomes limiting. The soluble periplasmic cytochrome cd 1 does not contribute significantly to the total oxygen consumption rate, although its maximal catalytic capacity may be high. The fact thap the activity of alternative TMPD oxidase is not proportional to cytochrome o content is discussed in relation to possible occurrence of two distinct cytochrome o ‐type terminal oxidases.

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