# Administrative Supplement (Instrumentation) for R35 GM124908: Bioinorganic Chemistry of Nitrogen

> **NIH NIH R35** · CORNELL UNIVERSITY · 2024 · $72,285

## Abstract

Project Summary - Bioinorganic Chemistry of Nitrogen
 The long-term goal of the PI’s research program is to understand how biology uses transition metals to
control the speciation of redox-active substrates including reactive or “fixed” nitrogen species (RNS). Reactive
nitrogen species serve vital roles in biology. For example, nitric oxide (NO) is a cellular signaling agent that
regulates vasodilation in mammalian systems. In a separate context, nitrate (NO3–) can substitute for dioxygen
(O2) as the terminal electron acceptor during cellular respiration by bacteria that include human pathogens.
This proposal describes a continuation of efforts to elucidate mechanisms of the biogeochemical nitrogen cycle
via the study of metalloenzymes as well as model complexes that interconvert RNS. A key knowledge gap that
will be addressed through proteomics and enzymology concerns the means by which ammonia oxidizing
archaea derive chemical energy from the oxidation of hydroxylamine. The operative enzyme and the product of
this reaction remain unknown. Activity guided purification and mass spectrometry will furnish the identity of this
globally proliferated nitrogen cycle protein for subsequent characterization by spectroscopy, X-ray
crystallography, and kinetics. Further work will explore product selectivity in RNS oxidation biochemistry by
heme P460 proteins to determine how NO is selected over nitrous oxide (N2O) to differentiate metabolic from
detoxification proteins. The PI will continue to collaborate with leading bioinorganic chemists to understand
how transition metals prime RNS for oxidation or reduction and how selectivity in these reactions is achieved.
These collaborations will leverage the PI’s expertise in X-ray spectroscopic as well as in other inorganic
spectroscopies. Key examples of these collaborations involve site-selective spectroscopic probing of metal
atoms in the FeMo cofactor of nitrogenase, the means by which multicopper clusters reduce N2O, and studying
the electronic structures and reactivities of Lewis-acid stabilized RNS that have been rendered capable of
undergoing redox transformations independent of proton transfer.

## Key facts

- **NIH application ID:** 11098968
- **Project number:** 3R35GM124908-07S1
- **Recipient organization:** CORNELL UNIVERSITY
- **Principal Investigator:** Kyle M Lancaster
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $72,285
- **Award type:** 3
- **Project period:** 2017-09-15 → 2028-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/11098968

## Citation

> US National Institutes of Health, RePORTER application 11098968, Administrative Supplement (Instrumentation) for R35 GM124908: Bioinorganic Chemistry of Nitrogen (3R35GM124908-07S1). Retrieved via AI Analytics 2026-05-22 from https://api.ai-analytics.org/grant/nih/11098968. Licensed CC0.

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