dc.creatorLewis Ballester, Ariel
dc.creatorBatabyal, Dipanwita
dc.creatorEgawa, T.
dc.creatorLu, Changyuan
dc.creatorLin, Yu
dc.creatorMarti, Marcelo Adrian
dc.creatorCapece, Luciana
dc.creatorEstrin, Dario Ariel
dc.creatorYeh, S. R.
dc.date.accessioned2020-05-04T14:49:42Z
dc.date.accessioned2022-10-15T14:56:31Z
dc.date.available2020-05-04T14:49:42Z
dc.date.available2022-10-15T14:56:31Z
dc.date.created2020-05-04T14:49:42Z
dc.date.issued2009-09
dc.identifierLewis Ballester, Ariel; Batabyal, Dipanwita; Egawa, T.; Lu, Changyuan; Lin, Yu; et al.; Evidence for a ferryl intermediate in a heme-based dioxygenase; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 106; 41; 9-2009; 17371-17376
dc.identifier0027-8424
dc.identifierhttp://hdl.handle.net/11336/104129
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4399425
dc.description.abstractIn contrast to the wide spectrum of cytochrome P450 monooxygenases, there are only 2 heme-based dioxygenases in humans: tryptophan dioxygenase (hTDO) and indoleamine 2,3-dioxygenase (hIDO). hTDO and hIDO catalyze the same oxidative ring cleavage reaction of L-tryptophan to N-formyl kynurenine, the initial and rate-limiting step of the kynurenine pathway. Despite immense interest, the mechanism by which the 2 enzymes execute the dioxygenase reaction remains elusive. Here, we report experimental evidence for a key ferryl intermediate of hIDO that supports a mechanism in which the 2 atoms of dioxygen are inserted into the substrate via a consecutive 2-step reaction. This finding introduces a paradigm shift in our understanding of the heme-based dioxygenase chemistry, which was previously believed to proceed via simultaneous incorporation of both atoms of dioxygen into the substrate. The ferryl intermediate is not observable during the hTDO reaction, highlighting the structural differences between the 2 dioxygenases, as well as the importance of stereoelectronic factors in modulating the reactions.
dc.languageeng
dc.publisherNational Academy of Sciences
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/106/41/17371
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.0906655106
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectIndoleamine 2,3-Dioxygenase
dc.subjectQm-Mm
dc.subjectResonance Raman Spectroscopy
dc.titleEvidence for a ferryl intermediate in a heme-based dioxygenase
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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