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NOBEL PRIZE 2026

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NIHNATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESR01

Heme-Dependent Chemistry in Aromatic Oxidation

Completed
Institution
UNIVERSITY OF TEXAS SAN ANTONIO, TX
Principal investigator
Aimin Liu
Funding
$324K
Duration
2014–2026
Open portfolio

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Abstract

Heme-Dependent Chemistry in Aromatic Oxidation Abstract Heme-containing enzymes are ubiquitous, contributing to various processes and catalyzing a vast array of oxidative chemistries. Histidine-ligated heme enzymes, such as the heme-dependent aromatic oxygenase (HDAO) superfamily, can use either molecular oxygen or hydrogen peroxide to oxidize their substrates. What is currently not understood are the molecular factors that engender these enzymes with their respective specificities, i.e., after generation of the critical active oxidant, how is a single reaction type catalyzed. The answer to this question will broaden our fundamental understanding of enzyme catalysis, de novo enzyme design, and protein engineering. This application focuses on the structural and mechanistic characterization of three aromatic-oxidizing enzymes of the HDAO superfamily that are involved in natural product and antimicrobial drug biosynthesis: TyrH, SfmD, and MarE. TyrH is a group of heme-dependent L-DOPA forming monooxygenase in the biosynthesis of antibiotics with a pyrroline moiety. SfmD mediates the regioselective hydroxylation of 3-methyl-L-tyrosine for synthesizing the core quinone structure of saframycin A. MarE forms an oxindole structure for many compounds. These enzymes play important roles in the biosynthetic pathway of secondary metabolites found in many biologically active natural products and pharmaceutical lead compounds. Our primary goal is to understand the key factors that govern their hydroxylation mechanisms and their differing strategies to form oxidizing intermediates with these enzymes. We have utilized a broad spectrum of approaches to probe the intricate molecular details of these enzyme mechanisms using noncanonical amino acids, substrate analogs, time-resolved UV-vis and EPR spectroscopies, kinetics, and isotope-labeling studies, and we have been successful trapping on-pathway reaction intermediates in crystallo. The proposed work will test our hypotheses regarding i) how the heme-based oxidant is generated, ii) how oxygen is directed to the substrate, and iii) unravel the structural factors that affect catalysis. The outcome of the proposed studies is an in-depth understanding of these three related catalytic systems to aid the development of scaffolds for rational drug design and discovery processes.

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R01NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESSpecial Emphasis Panel[ZRG1-BCMB-V(02)M]enzymesenzymeintermediatesbiosynthesiscatalysissuperfamilyaromaticoxidant

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