#133: Deciphering tryptophan oxygenation: Key modulators of 2-oxindole formation in MarE (Nguyen) https://doi.org/10.1002/anie.202510848
#132: Robust error calibration for serial crystallography (Mittan-Moreau) https://doi.org/10.1107/S2059798325002852
#131: Protein-derived cofactors: Chemical innovations expanding enzyme catalysis (Graciano) https://doi.org/10.1039/d4cs00981a
#130: Catalase-peroxidase (KatG): A potential frontier in tuberculosis drug development (Liu) https://doi.org/10.1080/10409238.2025.2470630
#129: Structural insights into 2-oxindole-forming monooxygenase MarE (Shin) https://doi.org/10.1080/10409238.2025.2470630
#128: ACMSD catalyzes enol/keto tautomerization of oxaloacetate (Yang ) https://doi.org/10.1016/j.jbc.2024.107878
#127: Indole-N-linked hydroperoxyl adduct of protein-derived cofactor modulating KatG functions (Li) https://onlinelibrary.wiley.com/doi/epdf/10.1002/anie.202407018
#126: Cobalt(II)-substituted cysteamine dioxygenase oxygenation ... (Li) https://Feradical.utsa.edu/labdoc/JACS2024_Co(II)-ADO.pdf
#125: Unveiling the mechanism of cysteamine dioxygenase ... (Duan) https://Feradical.utsa.edu/labdoc/MIE2024_ADO.pdf
#124: In situ structural observation of a ... (Nguyen) https://Feradical.utsa.edu/labdoc/JACS23_CYP121_cpd0.pdf
#123: Structural and spectroscopic characterization of RufO ... (Jordan) https://Feradical.utsa.edu/labdoc/JBC23_RufO.pdf
#122: Simultaneous separation and detection of nine kynurenine pathway metabolites ... (Patel) https://Feradical.utsa.edu/labdoc/ACA23_KYN_Metabolites.pdf
#121: Structural insights into the half-of-sites reactivity ... (Nguyen) https://Feradical.utsa.edu/labdoc/COSB2023_half-of-sites_reactivity.pdf
#120: Kynurenine pathway regulation at its critical junctions with fluctuation of tryptophan (Newton) https://Feradical.utsa.edu/labdoc/Metabolites-13040500.pdf
#119: Quantitation of tryptophan and kynurenine in human plasma ... (Patel) https://Feradical.utsa.edu/labdoc/Electrophoresis2023.pdf
#118: Charge maintenance during catalysis in non-heme iron oxygenases (Traore) https://Feradical.utsa.edu/labdoc/ACSCatal2022_Charge-Maintenance.pdf
#117: Probing extradiol dioxygenase mechanism in NAD biosynthesis ... (Davis) https://Feradical.utsa.edu/labdoc/EIBC2022_HAO.pdf
#116: Metalloenzymes involved in carotenoid biosynthesis in plants (Davis) https://Feradical.utsa.edu/labdoc/MiE202201012.pdf
#115: A new regime of heme-dependent aromatic oxygenase superfamily (Shin) https://Feradical.utsa.edu/labdoc/PNAS2021_HDAO.pdf
#114: Crystal structure of human cysteamine dioxygenase (Wang) https://Feradical.utsa.edu/labdoc/JBC2021_ADO.pdf
#113: HygY is a twitch radical SAM epimerase with latent dehydrogenase activity... (Besandre) https://Feradical.utsa.edu/labdoc/jacs.1c05727_HygY.pdf
#112: Capillary electrochromatography-mass spectrometry of kynurenine pathway metabolites (Chawdhury) https://Feradical.utsa.edu/labdoc/JChromatogrA_2021.pdf
#111: Molecular rationale for partitioning between C-H and C-F bond activation ... (Wang) https://Feradical.utsa.edu/labdoc/jacs.1c00175_TyrH.pdf
#110: A novel catalytic heme cofactor in SfmD with a single thioether bond and a bis-His ligand set ... (Shin) http://feradical.utsa.edu/labdoc/ChemSci2021_SfmD.pdf
#109: Heme binding to HupZ with a C-terminal tag from Group A Strep (Traore) https://Feradical.utsa.edu/labdoc/Molecules2021_HupZ.pdf
#108: Diflunisal derivatives as modulators of ACMSD of kynurenine pathway (Yang) https://Feradical.utsa.edu/labdoc/JMC2021_ACMSD.pdf
#107: Formation of monofluorinated radical cofactor in galactose oxidase ... (Li) https://Feradical.utsa.edu/labdoc/JACS2020_GAO.pdf
#106: Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens (Wnag) https://Feradical.utsa.edu/labdoc/PNAS2020_HAO_intermediates.pdf
#105: Characterization of the non-heme iron center of cysteamine dioxygenase ... (Wnag) https://Feradical.utsa.edu/labdoc/JBC2020_ADO.pdf
#104: Kinetic and spectroscopic characterization of the TDO catalytic ternary complex (Geng) https://Feradical.utsa.edu/labdoc/acs.biochem.0c00179_TDO.pdf
#103: Carbon-fluorine bond cleavage mediated by metalloenzymes (Wang) https://Feradical.utsa.edu/labdoc/CSR_c9cs00740g.pdf
#102: Substrate-assisted hydroxylation and O-demethylation in peroxidase-like CYP121 (Nguyen) https://feradical.utsa.edu/labdoc/acscatal.9b04596_CYP121.pdf
#101: Crystal structures of L-DOPA dioxygenase (Wang) https://Feradical.utsa.edu/labdoc/acs.biochem.9b00396_ssDDO.pdf
#100: Quaternary structure of ACMSD controls its activity (Yang) https://Feradical.utsa.edu/labdoc/JBC2019-SAXS.pdf
#99: Biocatalytic carbon-hydrogen and carbon-fluorine bond cleavage through hydroxylation ... (Wang) https://Feradical.utsa.edu/labdoc/acscatal.9b00231_TyrH.pdf
#98: Probing the Cys-Tyr cofactor biogenesis in cysteine dioxygenase ... (Li) https://Feradical.utsa.edu/labdoc/ACS.Biochem.9b00006_CDO.pdf
#97: Cleavage of a carbon-fluorine bond by an engineered cysteine dioxygenase (Li) https://Feradical.utsa.edu/labdoc/NatChemBio2018_CDO.pdf
#96: Backbone dehydrogenation in pyrrole-based pincer ligands (Krishnan) https://Feradical.utsa.edu/labdoc/IC2018_Pincer.pdf
#95: Adapting to oxygen: HAO employs loop dynamics to accommodate ... (Yang) https://Feradical.utsa.edu/labdoc/JBC2018s_HAO.pdf
#94: Cofactor biogenesis in cysteamine dioxygenase ... (Wang) https://Feradical.utsa.edu/labdoc/Angewandte_Chemie_2018_ADO.pdf
#93: Reassignment of the human aldehyde dehydrogenase ALDH8A1 ... (Davis) https://Feradical.utsa.edu/labdoc/JBC2018-AMSDH.pdf
#92: Stepwise O-atom transfer in heme-based TDO ... (Shin) https://Feradical.utsa.edu/labdoc/JACS2018_TDO.pdf
#91: High-frequency/high-field EPR and theoretical studies of Trp-based radicals (Davis) https://Feradical.utsa.edu/labdoc/JPC_2018_Trp_Radicals.pdf
#90: Radical trapping study of the relaxation of bis-Fe(IV) MauG (Davis) https://Feradical.utsa.edu/labdoc/ROS2018_MauG.pdf
#89: Probing ligand exchange in the P450 enzyme CYP121 ... (Fielding) https://feradical.utsa.edu/labdoc/JACS2017_CYP121.pdf
#88: Mutual synergy between catalase and peroxidase activities of Mtb KatG ... (Njuma) https://Feradical.utsa.edu/labdoc/JBC2017_KatG.pdf
#87: Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 ... (Dornevil) https://Feradical.utsa.edu/labdoc/JBC2017-CYP121.pdf
#86: Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency (Ferreira) https://Feradical.utsa.edu/labdoc/MGM2017_Hypertryptophanemia.pdf
#85: Oxygen activation by nonheme iron dioxygenases involved in the degradation of aromatics (Wang) https://Feradical.utsa.edu/labdoc/JBIC2017_NonhemeFe.pdf
#84: Heterolytic O-O bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG (Geng) https://Feradical.utsa.edu/labdoc/JIB_MauG_Glu113.pdf
#83: A pitcher-and-catcher mechanism drives endogenous substrate isomerization ... (Yang) https://Feradical.utsa.edu/labdoc/JBC2016_Dehydrogenase.pdf
#82: Control of carotenoid biosynthesis through a heme-based cis-trans isomerase (Beltran) https://Feradical.utsa.edu/labdoc/NatChemBio2015_Z-ISO.pdf
#81: What is the tryptophan kynurenine pathway and why is it important to neurotherapeutics? (Davis) https://Feradical.utsa.edu/labdoc/ERN20150019-Kynurenine.pdf
#80: An iron reservoir to the catalytic metal: The rubredoxin iron in an extradiol dioxygenase (Liu) https://Feradical.utsa.edu/labdoc/JBC2015-TwoMetals.pdf
#79: Probing bis-Fe(IV) MauG: Experimental evidence for the long-range charge-resonance model (Geng) https://Feradical.utsa.edu/labdoc/Angewandte2015_MauG_CR.pdf
#78: Crystallographic and spectroscopic snapshots reveal a dehydrogenase in action (Huo) https://Feradical.utsa.edu/labdoc/ncomms6935.pdf
#77: Human (ACMSD): A structural and mechanistic unveiling (Huo) https://Feradical.utsa.edu/labdoc/Proteins2014-hACMSD.pdf
#76: Bis-Fe(IV): Nature's sniper for long-range oxidation (Geng) https://Feradical.utsa.edu/labdoc/JBIC2014-Sniper.pdf
#75: Amidohydrolase Superfamily (Liu) https://Feradical.utsa.edu/labdoc/ELS_Amidohydrolase_Superfamily.pdf
#74: Heme-dependent dioxygenases in tryptophan oxidation (Geng) https://Feradical.utsa.edu/labdoc/ABB2014-TDO.pdf
#73: The Power of two: Arginine 51 and arginine 239* from a neighboring subunit are essential ... (Huo) https://Feradical.utsa.edu/labdoc/JBC2013_Power2.pdf
#72: Pirin is an iron-dependent redox regulator of NF-?B (Liu) https://Feradical.utsa.edu/labdoc/PNAS2013_Pirin.pdf
#71: Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG (Geng) https://Feradical.utsa.edu/labdoc/PNAS-2013-CR-MauG.pdf
#70: Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis (Yukl) https://Feradical.utsa.edu/labdoc/PNAS-2013-Trp-Diradical.pdf
#69: Development of a CZE-ESI-MS assay for profiling picolinic acid and quinolinic acid ... (Wang) https://feradical.utsa.edu/labdoc/Electrophoresis-2013.pdf
#68: An unexpected copper catalyzed 'reduction' of an arylazide to amine ... (Peng) https://Feradical.utsa.edu/labdoc/Tetrahedron2013_Nitrene.pdf
#67: Improved separation and detection of picolinic acid and quinolinic acid by ... (Wang) https://Feradical.utsa.edu/labdoc/JChrom2013.pdf
#66: Chemical rescue of the distal histidine mutants of tryptophan 2,3-dioxygenase (Geng) https://Feradical.utsa.edu/labdoc/JACS2012_TDO.pdf
#65: Evidence for a dual role of an active site histidine in ACMSD (Huo) https://Feradical.utsa.edu/labdoc/BI2012_ACMSD.pdf
#64: Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on ... (Tarboush) https://Feradical.utsa.edu/labdoc/FEBS_Letters_2012.pdf
#63: Decarboxylation mechanisms in biological system (Li) https://Feradical.utsa.edu/labdoc/BO12_Decarboxylation.pdf
#62: The role of calcium in metalloenzyme ... (Chen) https://Feradical.utsa.edu/labdoc/BI2012_Calcium_MauG.pdf
#61: Tryptophan tryptophylquinone biosynthesis ... (Davidson) https://Feradical.utsa.edu/labdoc/BBA2012_MauG-review.pdf
#60: Proline 107 is a major determinant in maintaining ... (Feng) https://Feradical.utsa.edu/labdoc/BI2012_Pro107.pdf
#59: The roles of Rhodobacter sphaeroides copper chaperones ... (Thompson) https://Feradical.utsa.edu/labdoc/BBA2012_CcO.pdf
#58: Synthesis, characterisation, and preliminary in vitro studies of vanadium(IV) complexes ... (Lewis) https://Feradical.utsa.edu/labdoc/EJIC2012-Vanadium.pdf
#57: Mutagenesis of tryptophan199 suggests that electron hopping is required for ... (Tarboush) http://feradical.utsa.edu/labdoc/PNAS2011_Trp199.pdf
#56: The reactivation mechanism of tryptophan 2,3-dioxygenase by hydrogen peroxide (Fu) https://Feradical.utsa.edu/labdoc/JBC2011_TDO.pdf
#55: Nature's strategy for oxidizing tryptophan: EPR and Mossbauer ... (Dornevil) https://Feradical.utsa.edu/labdoc/ch15.pdf
#54: Redox and oxygen sensing in the regulation of transcription by metalloproteins (Rehmani) https://Feradical.utsa.edu/labdoc/ch8.pdf
#53: The tightly bound calcium of MauG is required for ... (Shin) https://feradical.utsa.edu/labdoc/BI2011_Ca.pdf
#52: Proline 96 of the copper ligand loop of amicyanin regulates electron transfer ... (Choi) https://Feradical.utsa.edu/labdoc/BI2011_Pro96.pdf
#51: EPR and Mossbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase (Gupta) https://Feradical.utsa.edu/labdoc/JACS2010_TDO.pdf
#50: Mutagenic analysis of Cox11 of Rhodobacter sphaeroides ... (Thompson) https://Feradical.utsa.edu/labdoc/BI2010_COX.pdf
#49: Heme iron nitrosyl complex of MauG reveals efficient redox equilibrium ... (Fu) https://Feradical.utsa.edu/labdoc/BI2009_MauG.pdf
#48: Electron Paramagnetic Resonance (EPR) in Enzymology (Liu) https://Feradical.utsa.edu/labdoc/WECB668_EPR-in-Enzymology.pdf
#47: A single EF-hand isolated from STIM1 forms dimer ... (Huang) https://Feradical.utsa.edu/labdoc/FEBSJ2009_EFhand.pdf
#46: Defining the role of the axial ligand of the type 1 copper site in amicyanin ... (Choi) https://Feradical.utsa.edu/labdoc/BI2009_Ami.pdf
#45: A catalytic di-heme bis-Fe(IV) form of MauG, Alternative to an Fe(IV)=O porphyrin radical (Li) https://Feradical.utsa.edu/labdoc/PNAS2008-bisFe4.pdf
#44: Kinetic and physical evidence that the di-heme enzyme MauG tightly binds to ... (Li) https://feradical.utsa.edu/labdoc/BI2008_MauG.pdf
#43: Purification and characterization of the epoxidase catalyzing the formation of fosfomycin ... (Munos) https://Feradical.utsa.edu/labdoc/BI2008_HppE.pdf
#42: Amidohydrolase Superfamily (Liu et al.) https://Feradical.utsa.edu/labdoc/eLS2007_Amidohydrolase.pdf
#41: Determination of the substrate binding mode to the active site iron of ... (Yan) https://Feradical.utsa.edu/labdoc/BI2007_HppE.pdf
#40: Detection of transient intermediates in decarboxylation catalyzed by ACMSD (Li) https://Feradical.utsa.edu/labdoc/JACS2007_ACMSD.pdf
#39: Crystallographic analysis of ACMS decarboxylase ... (Martynowski) https://Feradical.utsa.edu/labdoc/BI2006_NbaD_Structure.pdf
#38: Transition metal-catalyzed nonoxidative decarboxylation reactions (Liu) https://Feradical.utsa.edu/labdoc/BI2006_NewConcept.pdf
#37: ACMSD is a new member of the amidohydrolase superfamily (Li) https://feradical.utsa.edu/labdoc/BI2006_ACMSD.pdf
#36: The mechanism of inactivation of HAO by 4-chloro-3 hydroxyanthranilate (Colabroy) https://Feradical.utsa.edu/labdoc/BI2005_HAO.pdf
#35: Kinetic and spectroscopic characterization of ACMSD ... (Li) https://Feradical.utsa.edu/labdoc/JACS2005_ACMSD.pdf
Selected from publictaions prior to independent
#27: https://Feradical.utsa.edu/labdoc/PNAS2003_TauD.pdf
#25: https://Feradical.utsa.edu/labdoc/JACS2001_rRaman.pdf
#24: https://Feradical.utsa.edu/labdoc/JACS2001_TauD.pdf
#21: https://Feradical.utsa.edu/labdoc/PNAS2000_Yeast_RNR.pdf
#19: https://Feradical.utsa.edu/labdoc/JBC2000_aRNR.pdf
#18: https://Feradical.utsa.edu/labdoc/BI1998_Mtb_RNR.pdf