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Advanced Spectroscopic and Computational Analysis of Metal Sites in Enzymes, Biomimetic Models, and Catalytic Intermediates.

Award Number: R35GM141948
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

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Advanced Spectroscopic and Computational Analysis of Metal Sites in Enzymes, Biomimetic Models, and Catalytic Intermediates. Summary/Abstract Life of all organisms, including humans, depends on the activation of small stable molecules by metalloproteins to provide selective and rapid chemical transformations. The goal of the proposed research is to elucidate how specific metalloenzymes function by monitoring and analyzing the atomic level changes that occur at the metal active site during the reaction. These studies are augmented with benchmark studies of biomimetic complexes. The understanding gleaned from this work will provide a molecular basis for finding causes and remedies of diseases. The focus of the research efforts will be on how the interfacing of the active sites in metalloproteins with the protein matrix affects enzymatic function. The primary atomic coordination to the metal is of critical importance, but in many cases, weaker secondary sphere interactions, usually hydrogen bonds from nearby amino acid residues can have significant influence as well. The investigations in our lab use advanced spectroscopic and computational methods, providing detailed characterizations of the metal active sites in proteins that can be compared with an extensive database of benchmarks that we and other researchers have gathered from synthetic model complexes over the years. To understand how an enzyme works, we study key steps in their chemical mechanism by trapping and characterizing reactive intermediates and tracking their elemental kinetics on a millisecond time scale. The work is highly collaborative as we depend on the expertise of many synthetic and biochemical research groups to ensure access to biomimetic and protein complexes that can be, through joint effort, prepared cleanly with well-defined protocols.


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: 2025 ( Subtotal = $0 )
2025	2024	CARNEGIE MELLON UNIVERSITY	5000 FORBES AVE	PITTSBURGH	PA	15213	ALLEGHENY	USA	Biomedical Research and Research Training	000	4	11/27/2024	NON-COMPETING CONTINUATION	$0
														Subtotal = $0

Issue Date FY: 2024 ( Subtotal = $277,541 )
2024	2024	CARNEGIE MELLON UNIVERSITY	5000 FORBES AVE	PITTSBURGH	PA	15213	ALLEGHENY	USA	Biomedical Research and Research Training	000	4	7/11/2024	NON-COMPETING CONTINUATION	$277,541
														Subtotal = $277,541

Issue Date FY: 2023 ( Subtotal = $277,059 )
2023	2023	CARNEGIE MELLON UNIVERSITY	5000 FORBES AVE	PITTSBURGH	PA	15213	ALLEGHENY	USA	Biomedical Research and Research Training	000	3	6/27/2023	NON-COMPETING CONTINUATION	$277,059
														Subtotal = $277,059

Issue Date FY: 2022 ( Subtotal = $276,591 )
2022	2022	CARNEGIE MELLON UNIVERSITY	5000 FORBES AVE	PITTSBURGH	PA	15213	ALLEGHENY	USA	Biomedical Research and Research Training	000	2	7/29/2022	NON-COMPETING CONTINUATION	$276,591
														Subtotal = $276,591

Issue Date FY: 2021 ( Subtotal = $406,751 )
2021	2021	CARNEGIE MELLON UNIVERSITY	5000 FORBES AVE	PITTSBURGH	PA	15213	ALLEGHENY	USA	Biomedical Research and Research Training	000	1	8/20/2021	NEW	$406,751
														Subtotal = $406,751

Grand Total All Awards = $1,237,942

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Advanced Spectroscopic and Computational Analysis of Metal Sites in Enzymes, Biomimetic Models, and Catalytic Intermediates.

Award Number: R35GM141948

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

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

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