Title : Cytochrome P-450 involvement in the NADPH-dependent lipid peroxidation in human placental mitochondria.

Pub. Date : 1990 May 1

PMID : 2160283






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Cytochrome P-450 involvement in the NADPH-dependent lipid peroxidation in human placental mitochondria. NADP cytochrome P450 family 4 subfamily F member 3 Homo sapiens
2 The NADPH-dependent lipid peroxidation in human placental mitochondria has been found to be inhibited strongly by amphenone B, aminoglutethimide and carbon monoxide, inhibitors of cytochrome P-450-mediated reactions, but was hardly affected by respiratory chain inhibitors. NADP cytochrome P450 family 4 subfamily F member 3 Homo sapiens
3 Cytochrome c, an exogenous electron acceptor which is known to compete with cytochrome P-450 for the reducing equivalents, showed an inhibitory effect on NADPH-dependent lipid peroxidation. NADP cytochrome P450 family 4 subfamily F member 3 Homo sapiens
4 These data provide evidence that cytochrome P-450 is involved in NADPH-dependent mitochondrial lipid peroxidation. NADP cytochrome P450 family 4 subfamily F member 3 Homo sapiens
5 It is suggested that superoxide liberated from cytochrome P-450, in combination with iron, may be responsible for initiation of NADPH-dependent lipid peroxidation in human placental mitochondria. NADP cytochrome P450 family 4 subfamily F member 3 Homo sapiens