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

> **NIH NIH R35** · CARNEGIE-MELLON UNIVERSITY · 2022 · $276,591

## Abstract

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.

## Key facts

- **NIH application ID:** 10472543
- **Project number:** 5R35GM141948-02
- **Recipient organization:** CARNEGIE-MELLON UNIVERSITY
- **Principal Investigator:** MICHAEL P HENDRICH
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2022
- **Award amount:** $276,591
- **Award type:** 5
- **Project period:** 2021-09-01 → 2026-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10472543

## Citation

> US National Institutes of Health, RePORTER application 10472543, Advanced Spectroscopic and Computational Analysis of Metal Sites in Enzymes, Biomimetic Models, and Catalytic Intermediates. (5R35GM141948-02). Retrieved via AI Analytics 2026-05-24 from https://api.ai-analytics.org/grant/nih/10472543. Licensed CC0.

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