A comparative study of heme degradation by NADPH-cytochrome c reductase alone and by the complete heme oxygenase system. Distinctive aspects of heme degradation by NADPH-cytochrome c reductase.
نویسندگان
چکیده
منابع مشابه
Presence of heme oxygenase and NADPH cytochrome P-450 (c) reductase in human corneal epithelium.
The presence of heme oxygenase and NADPH cytochrome P-450 (c) reductase, the latter an integral component of heme oxygenase and cytochrome P-450-dependent drug metabolizing enzymes, was demonstrated in human corneal epithelium. We reported for the first time that human corneal epithelium contains heme oxygenase activity as high as 20% of that reported for the human liver. Using immunological te...
متن کاملProtein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase.
Heme oxygenase (HO) catalyzes the rate-limiting step in the O2-dependent degradation of heme to biliverdin, CO, and iron with electrons delivered from NADPH via cytochrome P450 reductase (CPR). Biliverdin reductase (BVR) then catalyzes conversion of biliverdin to bilirubin. We describe mutagenesis combined with kinetic, spectroscopic (fluorescence and NMR), surface plasmon resonance, cross-link...
متن کاملFeatures of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system.
The heme oxygenase system was reconstituted from a heme oxygenase preparation highly purified from pig spleen microsomes and a partially purified NADPHcytochrome c reductase from pig liver microsomes. In the reconstituted heme oxygenase reaction, the relationship between the rate of heme degradation and the heme concentration was sigmoidal, and the heme concentration which gave the half-maximum...
متن کاملControl of DegP-dependent degradation of c-type cytochromes by heme and the cytochrome c maturation system in Escherichia coli.
c-Type cytochromes are located partially or completely in the periplasm of gram-negative bacteria, and the heme prosthetic group is covalently bound to the protein. The cytochrome c maturation (Ccm) multiprotein system is required for transport of heme to the periplasm and its covalent linkage to the peptide. Other cytochromes and hemoglobins contain a noncovalently bound heme and do not requir...
متن کاملCytochrome P450 2S1 is reduced by NADPH-cytochrome P450 reductase.
Cytochrome P450 (P450) 2S1 is one of the orphan P450s without a clear physiological function. Controversy has arisen as to whether it can interact with NADPH-P450 reductase and accept electrons. The reduction of 1,4-bis{[2-(dimethylamino-N-oxide)ethyl]amino}-5,8-dihydroxyanthracene-9,10-dione (AQ4N) by P450 2S1 was confirmed, and the NADPH consumption rates were measured aerobically and anaerob...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)34451-x