# Spectroscopy of Fe-S Cluster Proteins -- Information for Structure and Function - A Cryocooler Equipment Supplement

> **NIH NIH R01** · SETI INSTITUTE · 2024 · $58,020

## Abstract

GM65440 Supplement Project Summary
 The element iron plays an enormous role in biology, including electron transport reactions
(ferredoxins), oxygen transport and storage (hemoglobin and myoglobin), catalysis
(nitrogenase, P-450, hydrogenase, and thousands of other enzymes), small molecule sensing
(especially O2, CO, and NO), and DNA processing and repair. The health-relatedness of a better
understanding of the structure and function of biological Fe is clear.
 The general theme of research in the Cramer lab involves the use spectroscopy as a tool for
characterization of metals in biological systems. Much of this work involves the application of
synchrotron radiation x-ray sources. Thanks to enormous improvements of these sources,
experiments with exquisite sensitivity can now be conducted on dilute Fe samples. This includes
the technique Nuclear Resonance Vibrational Spectroscopy (NRVS), which is sensitive to the
motion of 57Fe in a sample. The x-ray experiments at international facilities are complemented
by IR and Raman measurements at the home lab.
 Pump-probe spectroscopy of sample in cryosolvents at temperatures down to -100°C and
also at temperatures close to 4 Kelvin is a major part of this project. A Nd:YAG OPO combination
will be used to pump the sample (initiate photochemistry) and a quantum cascade laser (QCL)
or FT-IR will be used to probe the subsequent reaction products.
 A cryostat for conducting experiments down to 4 Kelvin is essential for this work.
The goals for the remaining 2 years can be divided into 2 major themes:
· better understanding of the catalytic intermediates of the enzymes that process hydrogen –
 [NiFe] and [FeFe] hydrogenases, and
· information about structural changes that occur when Fe-S cluster proteins sense their
 environment, including mitoNEET and NAF-1, two health-related proteins which sense and
 communicate pH and redox status.
 The overall vision of this research program is to use spectroscopic methods to better
understand how iron is used in important proteins, in ways that complement the information
that can be gathered from diffraction and microscopy. In the course of research on specific
topics, spectroscopic techniques will be further developed for the bioinorganic community.

## Key facts

- **NIH application ID:** 11101066
- **Project number:** 3R01GM065440-20S1
- **Recipient organization:** SETI INSTITUTE
- **Principal Investigator:** Stephen P. Cramer
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $58,020
- **Award type:** 3
- **Project period:** 2002-03-01 → 2026-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/11101066

## Citation

> US National Institutes of Health, RePORTER application 11101066, Spectroscopy of Fe-S Cluster Proteins -- Information for Structure and Function - A Cryocooler Equipment Supplement (3R01GM065440-20S1). Retrieved via AI Analytics 2026-06-11 from https://api.ai-analytics.org/grant/nih/11101066. Licensed CC0.

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