# Nitrosative stress and NO detoxifying reaction mechanisms in microbial nonheme diiron proteins

> **NIH NIH R01** · OREGON HEALTH & SCIENCE UNIVERSITY · 2024 · $323,400

## Abstract

PROJECT SUMMARY
Metalloenzymes play crucial roles throughout human health and govern the biochemistry of dioxygen (O2) and
nitric oxide (NO). Pathogenic organisms depend on heme and nonheme iron-containing proteins to counter the
human immune response and to survive exposure to high concentrations of reactive oxygen and nitrogen
species (ROS/RNS). The Moënne-Loccoz Lab combines classic biochemical techniques, resonance Raman
(RR), FTIR, and EPR spectroscopies with time-resolved techniques to probe microbial enzymatic systems
characterized by X-ray crystallography, but with catalytic strategies that remain poorly understood or totally
unknown. In this project, a recent crystal structure of a novel mycobacterial diiron protein upregulated upon
macrophage infection is targeted for investigation after showing unique structural features and reactivity toward
RNS never seen before in biology or inorganic chemistry.

## Key facts

- **NIH application ID:** 10810778
- **Project number:** 5R01GM147588-02
- **Recipient organization:** OREGON HEALTH & SCIENCE UNIVERSITY
- **Principal Investigator:** PIERRE MOENNE-LOCCOZ
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $323,400
- **Award type:** 5
- **Project period:** 2023-04-01 → 2027-02-28

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10810778

## Citation

> US National Institutes of Health, RePORTER application 10810778, Nitrosative stress and NO detoxifying reaction mechanisms in microbial nonheme diiron proteins (5R01GM147588-02). Retrieved via AI Analytics 2026-05-27 from https://api.ai-analytics.org/grant/nih/10810778. Licensed CC0.

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