# Structures and Mechanisms of Iron-Sulfur Proteins in Redox Control and Stress Response

> **NIH NIH R35** · UNIVERSITY OF NEBRASKA LINCOLN · 2024 · $18,312

## Abstract

PROJECT SUMMARY
Iron-sulfur (Fe-S) clusters are ancient cofactors composed of multiple iron and sulfur atoms. Owing to the rich,
tunable redox reactivity and selectivity of the cluster, Fe-S proteins play multifaced roles in redox control under
both physiological and stress conditions, which is required for maintaining normal cellular functions and cell
survival. Thus, Fe-S proteins are tightly linked to health and diseases (such as cancer, diabetes, and bacterial
infection) in humans. The parent Maximizing Investigators’ Research Award (MIRA; R35 GM138157) project
addresses the critical gaps in structural and mechanistic understanding of Fe-S proteins in the cellular control of
redox homeostasis, including: i) the structural basis of redox reactivity and ligand selectivity in Fe-S clusters; ii)
the mechanism by which the redox state and integrity of the Fe-S cluster allows these proteins to sense redox
states and regulate transcription; iii) the structural biochemistry of Fe-S cluster biosynthesis and regulation; and
iv) the role of non-proteinaceous thiols in modulating Fe-S cluster-mediated redox control. The research goals
and approaches of the parent project are demonstrated in the three selected Fe-S protein-mediated mechanisms
for redox control and stress response in mycobacteria: i) redox sensing and transcriptional regulation by the
WhiB-like (Wbl) family proteins; ii) assembly, transfer, and repair of Fe-S clusters by the sulfur utilization factor
(SUF) system; and iii) mycothiol in Fe-S cluster homeostasis.
This diversity supplement request is to support the research training and career development of the pre-doctoral
candidate Daisy Guiza Beltran. Daisy’s long-term goal is to establish a research career in molecular mechanisms
of diseases. She has already gained skills in protein crystallography and protein biochemistry during her
undergraduate research and the first three years of her Ph.D. thesis research in the PI’s group. The proposed
research experience will expand Daisy’s expertise in structural biology and develop interdisciplinary skills in
biomedical sciences. The training activities will further enhance her leadership and communication abilities and
allow her to build a strong network of collaborations. The postdoctoral fellowship application will provide her with
an opportunity to further her research skills and career development. Additionally, her commitment to promoting
diversity and inclusion in the research environment will create a supportive and welcoming community for all,
which will help her become a successful and impactful researcher.

## Key facts

- **NIH application ID:** 10834378
- **Project number:** 3R35GM138157-04S1
- **Recipient organization:** UNIVERSITY OF NEBRASKA LINCOLN
- **Principal Investigator:** Limei Zhang
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $18,312
- **Award type:** 3
- **Project period:** 2020-09-01 → 2025-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10834378

## Citation

> US National Institutes of Health, RePORTER application 10834378, Structures and Mechanisms of Iron-Sulfur Proteins in Redox Control and Stress Response (3R35GM138157-04S1). Retrieved via AI Analytics 2026-05-26 from https://api.ai-analytics.org/grant/nih/10834378. Licensed CC0.

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