Title : Superoxide production by cytochrome b559. Mechanism of cytosol-independent activation.

Pub. Date : 1994 Feb 7

PMID : 8307196






4 Functional Relationships(s)
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1 It is shown that, depending on the composition of the phospholipid environment, cytochrome b599 binds FAD with high or low affinity, this being accompanied by changes in flavin absorbance and fluorescence. Flavin-Adenine Dinucleotide mitochondrially encoded cytochrome b Homo sapiens
2 High affinity binding of FAD to cytochrome b559 relipidated with phosphatidylcholine combined with phosphatidic acid is associated with an enhanced NADPH-driven O2- producing capacity. Flavin-Adenine Dinucleotide mitochondrially encoded cytochrome b Homo sapiens
3 A kinetic study of O2- production by cytochrome b559 reflavinated under stoichiometric FAD binding conditions revealed an FAD/heme ratio of 1:2. Flavin-Adenine Dinucleotide mitochondrially encoded cytochrome b Homo sapiens
4 A kinetic study of O2- production by cytochrome b559 reflavinated under stoichiometric FAD binding conditions revealed an FAD/heme ratio of 1:2. Flavin-Adenine Dinucleotide mitochondrially encoded cytochrome b Homo sapiens