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Cytochrome P450 enzymes: understanding the biochemical hieroglyphs

Author(s): Groves, John T.

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dc.contributor.authorGroves, John T.-
dc.date.accessioned2020-11-12T18:51:26Z-
dc.date.available2020-11-12T18:51:26Z-
dc.identifier.citationGroves, John T. (Cytochrome P450 enzymes: understanding the biochemical hieroglyphs. F1000Research, 10.12688/f1000research.6314.1en_US
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr18g0s-
dc.descriptionF1000Research. Volume 4, July 01, 2015, Article number 178.en_US
dc.description.abstractCytochrome 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. © 2015 Groves J.T.en_US
dc.format.extent4:178-1 - 178-8en_US
dc.language.isoen_USen_US
dc.relation.ispartofF1000Researchen_US
dc.rightsFinal published version. This is an open access article.en_US
dc.titleCytochrome P450 enzymes: understanding the biochemical hieroglyphsen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.12688/f1000research.6314.1-
dc.date.eissued2015-07-01en_US
dc.identifier.eissn2046-1402-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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