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The cytochrome b of the sea urchin Paracentrotus lividus is naturally resistant to myxothiazol and mucidin
Author(s) -
Esposti M.Degli,
Ghelli A.,
Butler G.,
Roberti M.,
Mustich A.,
Cantatore P.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81384-z
Subject(s) - paracentrotus lividus , sea urchin , ubiquinol , biology , biochemistry , reductase , cytochrome c1 , alanine , coenzyme q – cytochrome c reductase , mitochondrion , amino acid , cytochrome c , enzyme , microbiology and biotechnology
The ubiquinol:cytochrome c reductase activity of Paracentrotus lividus mitochondria is relatively insensitive to the specific inhibitors myxothiazol and mucidin. The I 50 of myxothiazol and mucidin are three and two orders of magnitude higher, respectively, in P. lividus than in bovine heart mitochondria. The natural resistance of the P. lividus reductase to these inhibitors can be correlated with a single amino replacement, an alanine for a glycine at position 143, in the sequence of cytochrome b . This position is located in a conserved region of the molecule, believed to be important in the oxidation of ubiquinol by the reductase.