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Title: Nitrogenase Inspired Peptide-Functionalized Catalyst for Efficient, Emission-Free Ammonia Production

Abstract

Ammonia production is one of the most important industrial processes in the world, as the major component of fertilizer to sustain higher food production. It is also one of the most energy intensive and carbon intensive chemical processes worldwide, primarily due to the steam methane reforming step to produce hydrogen for the reaction. Currently, ammonia is produced via the Haber Bosch process, which requires high temperature and pressure, and has low equilibrium efficiency. Due to these reaction conditions, the process is most economical at extremely large scale (100,000s of tons per day). In order to enable more distributed production scales which better match with renewable energy input and sustainable reactant sources, alternative methods of ammonia synthesis are needed, which scale more effectively and economically. One such approach is electrochemical synthesis based on ion exchange membrane cells. Peptide templating to form catalyst nanoparticles of controlled size, combined with peptide surface adsorbtion to model the nitrogenase active site, was used to develop novel catalyst materials and deposit them on electrodes.

Authors:
 [1]; ORCiD logo [1];  [2];  [3]
  1. Proton Energy Systems, Inc, Wallingford, CT (United States)
  2. Case Western Reserve Univ., Cleveland, OH (United States)
  3. Univ. of Arkansas, Fayetteville, AR (United States)
Publication Date:
Research Org.:
Proton Energy Systems, Inc, Wallingford, CT (United States)
Sponsoring Org.:
USDOE Office of Energy Efficiency and Renewable Energy (EERE), Advanced Manufacturing Office (EE-5A); Univ. of Arkansas, Fayetteville, AR (United States); Case Western Reserve Univ., Cleveland, OH (United States)
OSTI Identifier:
1425441
Report Number(s):
DOE-PROTON-15956
DOE Contract Number:  
SC0015956
Type / Phase:
SBIR (Phase I)
Resource Type:
Technical Report
Resource Relation:
Related Information: N/A
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 42 ENGINEERING; Ammonia; anion exchange membranes; peptide templating; catalysis

Citation Formats

Gellett, Wayne, Ayers, Katherine, Renner, Julie, and Greenlee, Lauren. Nitrogenase Inspired Peptide-Functionalized Catalyst for Efficient, Emission-Free Ammonia Production. United States: N. p., 2017. Web.
Gellett, Wayne, Ayers, Katherine, Renner, Julie, & Greenlee, Lauren. Nitrogenase Inspired Peptide-Functionalized Catalyst for Efficient, Emission-Free Ammonia Production. United States.
Gellett, Wayne, Ayers, Katherine, Renner, Julie, and Greenlee, Lauren. Sun . "Nitrogenase Inspired Peptide-Functionalized Catalyst for Efficient, Emission-Free Ammonia Production". United States. doi:.
@article{osti_1425441,
title = {Nitrogenase Inspired Peptide-Functionalized Catalyst for Efficient, Emission-Free Ammonia Production},
author = {Gellett, Wayne and Ayers, Katherine and Renner, Julie and Greenlee, Lauren},
abstractNote = {Ammonia production is one of the most important industrial processes in the world, as the major component of fertilizer to sustain higher food production. It is also one of the most energy intensive and carbon intensive chemical processes worldwide, primarily due to the steam methane reforming step to produce hydrogen for the reaction. Currently, ammonia is produced via the Haber Bosch process, which requires high temperature and pressure, and has low equilibrium efficiency. Due to these reaction conditions, the process is most economical at extremely large scale (100,000s of tons per day). In order to enable more distributed production scales which better match with renewable energy input and sustainable reactant sources, alternative methods of ammonia synthesis are needed, which scale more effectively and economically. One such approach is electrochemical synthesis based on ion exchange membrane cells. Peptide templating to form catalyst nanoparticles of controlled size, combined with peptide surface adsorbtion to model the nitrogenase active site, was used to develop novel catalyst materials and deposit them on electrodes.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Sun Apr 30 00:00:00 EDT 2017},
month = {Sun Apr 30 00:00:00 EDT 2017}
}

Technical Report:
This technical report may be released as soon as March 12, 2022
Other availability
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