Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]

• Main Author: John T. Groves
• Format: Article
• Language: English
• Published: F1000 Research Ltd 2015-07-01
• Series: F1000Research
• Subjects: Biocatalysis; Bioinorganic Chemistry; Biomacromolecule-Ligand Interactions; Cancer Therapeutics; Chemical Biology of the Cell; Drug Discovery & Design; Experimental Biophysical Methods; Protein Chemistry & Proteomics
• Online Access: http://f1000research.com/articles/4-178/v1

Cytochrome P450 (CYP) enzymes are the primary proteins of drug metabolism and steroid biosynthesis. These crucial proteins have long been known to harbor a cysteine thiolate bound to the heme iron. Recent advances in the field have illuminated the nature of reactive intermediates in the reaction cycle. Similar intermediates have been observed and characterized in novel heme-thiolate proteins of fungal origin. Insights from these discoveries have begun to solve the riddle of how enzyme biocatalyst design can afford a protein that can transform substrates that are more difficult to oxidize than the surrounding protein architecture.