Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens

Wang, Yifan; Liu, Kathy Fange; Yang, Yu; Davis, Ian; Liu, Aimin

doi:10.1073/pnas.2005327117

Title: Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens

Journal Article · Thu Jul 30 00:00:00 EDT 2020 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.2005327117· OSTI ID:1651144

^[1]; Liu, Kathy Fange ^[2]; Yang, Yu ^[1];

^[1];

^[1]

Univ. of Texas at San Antonio, TX (United States)
Univ. of Pennsylvania, Philadelphia, PA (United States)

The synthesis of quinolinic acid from tryptophan is a critical step in the de novo biosynthesis of nicotinamide adenine dinucleotide (NAD⁺) in mammals. Herein, the nonheme iron-based 3-hydroxyanthranilate-3,4-dioxygenase responsible for quinolinic acid production was studied by performing time-resolved in crystallo reactions monitored by UV-vis microspectroscopy, electron paramagnetic resonance (EPR) spectroscopy, and X-ray crystallography. Seven catalytic intermediates were kinetically and structurally resolved in the crystalline state, and each accompanies protein conformational changes at the active site. Among them, a monooxygenated, seven-membered lactone intermediate as a monodentate ligand of the iron center at 1.59-Å resolution was captured, which presumably corresponds to a substrate-based radical species observed by EPR using a slurry of small-sized single crystals. Other structural snapshots determined at around 2.0-Å resolution include monodentate and subsequently bidentate coordinated substrate, superoxo, alkylperoxo, and two metal-bound enol tautomers of the unstable dioxygenase product. These results reveal a detailed stepwise O-atom transfer dioxygenase mechanism along with potential isomerization activity that fine-tunes product profiling and affects the production of quinolinic acid at a junction of the metabolic pathway.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS); SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Sponsoring Organization:: National Science Foundation (NSF); National Institutes of Health (NIH); Lutcher Brown Endowment; USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institute of General Medical Sciences (NIGMS)

Grant/Contract Number:: CHE-1623856; CHE-1808637; GM108988; GM133721; MH107985; AC02-76SF00515; AC02-06CH11357; P41GM103393

OSTI ID:: 1651144

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Vol. 117, Issue 33; ISSN 0027-8424

Publisher:: National Academy of SciencesCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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