[HTML][HTML] The ONIOM method and its applications
The fields of theoretical and computational chemistry have come a long way since their
inception in the mid-20th century. Fifty years ago, only rudimentary approximations for very …
inception in the mid-20th century. Fifty years ago, only rudimentary approximations for very …
Structure and reaction mechanism in the heme dioxygenases
I Efimov, J Basran, SJ Thackray, S Handa… - Biochemistry, 2011 - ACS Publications
As members of the family of heme-dependent enzymes, the heme dioxygenases are
differentiated by virtue of their ability to catalyze the oxidation of l-tryptophan to N …
differentiated by virtue of their ability to catalyze the oxidation of l-tryptophan to N …
Trapping a cross-linked lysine–tryptophan radical in the catalytic cycle of the radical SAM enzyme SuiB
The radical S-adenosylmethionine (rSAM) enzyme SuiB catalyzes the formation of an
unusual carbon–carbon bond between the sidechains of lysine (Lys) and tryptophan (Trp) in …
unusual carbon–carbon bond between the sidechains of lysine (Lys) and tryptophan (Trp) in …
Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2, 3-dioxygenase
A Lewis-Ballester, F Forouhar, SM Kim, S Lew… - Scientific reports, 2016 - nature.com
Abstract Tryptophan 2, 3-dioxygenase (TDO) and indoleamine 2, 3-dioxygenase (IDO) play
a central role in tryptophan metabolism and are involved in many cellular and disease …
a central role in tryptophan metabolism and are involved in many cellular and disease …
The Mechanism of Formation of N-Formylkynurenine by Heme Dioxygenases
J Basran, I Efimov, N Chauhan… - Journal of the …, 2011 - ACS Publications
Heme dioxygenases catalyze the oxidation of l-tryptophan to N-formylkynurenine (NFK), the
first and rate-limiting step in tryptophan catabolism. Although recent progress has been …
first and rate-limiting step in tryptophan catabolism. Although recent progress has been …
ONIOM study on a missing piece in our understanding of heme chemistry: bacterial tryptophan 2, 3-dioxygenase with dual oxidants
Unique heme-containing tryptophan 2, 3-dioxygenase (TDO) and indoleamine 2, 3-
dioxygenase (IDO) catalyze oxidative cleavage of the pyrrole ring of l-tryptophan (Trp) …
dioxygenase (IDO) catalyze oxidative cleavage of the pyrrole ring of l-tryptophan (Trp) …
Complete reaction mechanism of indoleamine 2, 3-dioxygenase as revealed by QM/MM simulations
L Capece, A Lewis-Ballester, SR Yeh… - The Journal of …, 2012 - ACS Publications
Indoleamine 2, 3-dioxygenase (IDO) and tryptophan dioxygenase (TDO) are two heme
proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine (NFK) …
proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine (NFK) …
X-ray Emission Spectroscopy of Single Protein Crystals Yields Insights into Heme Enzyme Intermediates
S Emamian, KA Ireland, V Purohit… - The journal of …, 2022 - ACS Publications
Enzyme reactivity is often enhanced by changes in oxidation state, spin state, and metal–
ligand covalency of associated metallocofactors. The development of spectroscopic …
ligand covalency of associated metallocofactors. The development of spectroscopic …
Heme-dependent dioxygenases in tryptophan oxidation
Abstract l-Tryptophan is an essential amino acid for mammals. It is utilized not only for
protein synthesis but also for the biosynthesis of serotonin and melatonin by the serotonin …
protein synthesis but also for the biosynthesis of serotonin and melatonin by the serotonin …
The mechanism of substrate inhibition in human indoleamine 2, 3-dioxygenase
I Efimov, J Basran, X Sun, N Chauhan… - Journal of the …, 2012 - ACS Publications
Indoleamine 2, 3-dioxygenase catalyzes the O2-dependent oxidation of l-tryptophan (l-Trp)
to N-formylkynurenine (NFK) as part of the kynurenine pathway. Inhibition of enzyme activity …
to N-formylkynurenine (NFK) as part of the kynurenine pathway. Inhibition of enzyme activity …