Computational approaches to cytochrome P450 function

Sason Shaik*, Samuël P. De Visser

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

60 Scopus citations

Abstract

The action of cytochrome P450 (P450) enzymes has been for years a very active arena of research that led to important insights, and generated lively debates over the nature of the various species and their reactivity patterns1. The active species of the enzyme is based on an iron ligated to a protoporphyrin IX macrocycle and two additional axial ligands (Figure 2.1): one, called proximal, is a thiolate from a cysteinate side chain of the protein and the other, called distal, is a variable ligand that changes during the cycle. When the distal ligand becomes an oxo group, the species is called Compound I (Cpd I), which is the reactive species of the enzyme and one of the most potent oxidants known in nature.

Original languageEnglish
Title of host publicationCytochrome P450
Subtitle of host publicationStructure, Mechanism, and Biochemistry: Third edition
PublisherSpringer US
Pages45-85
Number of pages41
ISBN (Print)9780306483240
DOIs
StatePublished - 2005

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