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Functions and mechanisms of metalloenzymes in natural product and cofactor biosynthesis

Award Number: R35GM161291
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 03/10/2026
PERIOD OF PERFORMANCE END DATE: 12/31/2030

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Functions and mechanisms of metalloenzymes in natural product and cofactor biosynthesis - Abstract: Metalloenzymes frequently catalyze chemically challenging radical-mediated reactions necessary for the synthesis of the complex structures of natural products and cofactors. Their functional and mechanistic characterization has been a critical basis for the discovery and development of small molecule therapeutics, research probes, and biocatalysts. However, many metalloenzymes in natural product and cofactor biosynthetic pathways remain significantly under-explored because (1) characterization of metalloenzymes requires specialized expertise and techniques due to the unique reactivities and properties of their metallo- centers, (2) their substrates are frequently not readily available, and (3) their functions may not be apparent from their primary amino acid sequence or structural homologies. Consequently, many metalloenzymes remain under- or unexplored, leaving numerous mechanistic questions unanswered. The long-term goal of my group is to elucidate the mechanisms and functions of metalloenzymes in cofactor and natural product biosynthesis. This application combines two ongoing NIGMS R01 projects and focuses on O2-independent and dependent Fe enzymes: Radical S-adenosyl-L-methionine (rSAM) enzymes and non-heme iron-dependent oxygenases/oxidases. The proposed structural and mechanistic characterizations will reveal novel catalytic functions and mechanisms of (metallo)enzymes and address key questions in each enzyme family, including the mechanism of substrate-triggered radical initiation by rSAM enzymes and the mechanism of C-H or O-H activation by mono or dinuclear Fe cofactors. The results of these studies will uniquely bridge the knowledge gap between bioorganic and bioinorganic chemistry and broadly impact the fields of cofactor and natural product biosynthesis and metalloenzymology.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2026 ( Subtotal = $737,152 )
2026	2026	DUKE UNIVERSITY	2200 W MAIN ST	DURHAM	NC	27705	DURHAM	USA	Biomedical Research and Research Training	000	1	3/10/2026	NEW	$737,152
														Subtotal = $737,152

Grand Total All Awards = $737,152

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Functions and mechanisms of metalloenzymes in natural product and cofactor biosynthesis

Award Number: R35GM161291

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 03/10/2026

PERIOD OF PERFORMANCE END DATE: 12/31/2030

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