These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: [The role of heme in formation of the native structure of cytochrome P-450 LM2]. Author: Uvarov VIu, Tret'iakov VE, Kuznetsova GP, Archakov AI. Journal: Biokhimiia; 1990 Jan; 55(1):126-33. PubMed ID: 2344452. Abstract: The role of heme in the formation of cytochrome P-450 native structure was investigated. It was shown that treatment of purified and membrane-bound hemoproteins with H2O2 results in the total destruction of heme. After incubation with hemine the apoprotein thus obtained forms a catalytically active cytochrome P-450. The efficiency of this process depends on the enzyme microenvironment. The membrane-bound apoprotein may be reconstituted by 70-80%, whereas the soluble one--by 50%. It is concluded that the observed differences may be accounted for by a greater stability of the membrane-bound protein structure.[Abstract] [Full Text] [Related] [New Search]