Date of Award:
5-2016
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Chemistry and Biochemistry
Committee Chair(s)
Lance C. Seefeldt
Committee
Lance C. Seefeldt
Committee
Scott A. Ensign
Committee
Jeanette Norton
Abstract
One of the most important scientific advances in the last century was the Haber-Bosch process, the industrial process of fixing nitrogen from the atmosphere to ammonia. This allowed for the commercial production and sale of nitrogen for important uses such as fertilizer for farming. The Haber-Bosch process is partially credited with the population boom that has been seen in the last century and has greatly increased the standard of living in the developed world today. While this was a great scientific breakthrough, the cost of producing the required ammonia is high, and roughly 2% of worldwide energy is used annually to meet this demand. There are many microorganisms that can produce ammonia, known as diazotrophs, and indeed roughly half of all ammonia produced annually is produced by these microorganisms. Diazotrophs can fix nitrogen much more efficiently than our industrial process today, and research is being done to better understand the mechanism of biological nitrogen reduction.
The enzyme responsible for nitrogen fixation is known as nitrogenase, and has two component proteins. The MoFe protein is the catalytic enzyme and the Fe protein is the source of the electrons which provide the energy to reduce nitrogen. One of the key questions in nitrogenase catalysis is how the electrons that are provided by the Fe protein are transferred into and utilized by the MoFe protein to reduce nitrogen and produce ammonia. The goal of this thesis is to better understand how electrons travel through nitrogenase, and how they are utilized at the active site, FeMo-cofactor, when they arrive.
Checksum
594d5d2b7c4b52ac376f30a10aba48ea
Recommended Citation
Rasmussen, Andrew J., "Structural Insights into the Regulation of Electron Transfer in Nitrogenase, and Modulating the Reactivity of the Isolated Iron Molybdenum Cofactor" (2016). All Graduate Theses and Dissertations, Spring 1920 to Summer 2023. 4897.
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