Title : New cytochrome P450 mechanisms: implications for understanding molecular basis for drug toxicity at the level of the cytochrome.

Pub. Date : 2010 Jan

PMID : 19947890






1 Functional Relationships(s)
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1 AREAS COVERED IN THIS REVIEW: In this communication, attempts have been made to bring together past as well as present information indicating that i) the P450 active site has two differently accessible allosterically interacting subsites geared for entirely different types of functionally relevant interactions; and ii) substrate binding to the specific protein residues (Site I) forming the reducible high-spin complex and product binding at L(6) (Site II) of the heme iron forming inhibited low-spin complex can regulate the functional state of the enzyme during catalysis. Heme cytochrome P450 family 2 subfamily B member 6 Homo sapiens