The oxidative degradation of heme c by the microsomal heme oxygenase system.
نویسندگان
چکیده
منابع مشابه
Features 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 کاملMicrosomal Heme Oxygenase
This study characterizes microsomal heme oxygenase, a previously undescribed enzyme which catalyzes the oxidation of heme at the cr-methene bridge to form biliverdin. This step is then coupled with soluble NADPH-dependent biliverdin reductase to form bilirubin; microsomal heme oxygenase is rate-limiting in this pathway. By all analytical criteria, the product of this reaction is bilirubin. Most...
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The heme-heme oxygenase system has recently been recognized to possess important regulatory properties. It is tightly involved in both physiological as well as pathophysiological processes, such as cytoprotection, apoptosis, and inflammation. Heme functions as a double-edged sword. In moderate quantities and bound to protein, it forms an essential element for various biological processes, but w...
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Heme is ferrous protoporphyrin-IX that is the prosthetic group of hemoproteins, such as hemoglobin, myoglobin and cytochromes that are of vital importance. In contrast, “free heme”, a protein-unbound heme, that is either just synthesized but yet not incorporated into hemoproteins, or that is released from hemoprotein under oxidative conditions, is highly toxic, since it catalyzes the production...
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Heme oxygenase (HO) has been shown to be important for attenuating the overall production of reactive oxygen species (ROS) through its ability to degrade heme and to produce carbon monoxide (CO), biliverdin/bilirubin, and the release of free iron. Excess free heme catalyzes the formation of ROS, which may lead to endothelial cell (EC) dysfunction as seen in numerous pathological conditions incl...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)34452-1