Hydrogen Production by His Mutants of Artificial Hydrogenase

Wills, Emory Elizabeth (2019) Hydrogen Production by His Mutants of Artificial Hydrogenase. Undergraduate thesis, under the direction of Saumen Chakraborty from Chemistry & Biochemistry, University of Mississippi.

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Abstract

Nickel enzymes are relatively new to be studied, but they have been found to be useful in creating artificial hydrogenases. Nickel alone can be harmful, but when combined with proteins to create an enzyme, the hope is that through catalysts, hydrogen can be produced for viable energy. The proteins used in the experiments had respective mutations at points 113 and 26. The cysteine at both of these points was replaced by a histidine to hopefully enhance metal binding. To create artificial hydrogenases and produce energy, the proteins were induced by various metals including nickel, copper, and cobalt. After experimentation and analysis by UV spectroscopy, nickel was found to successfully stay bound to both C113H and C26H, and the proteins contained significant increases at the peaks of 280 nm which shows a higher concentration of protein. C26H and C113H when bound to copper and cobalt also showed increased peaks at 280 nm, increasing the protein concentrations drastically. Due to these increases, it is inherent that some catalytic activity occurred, but it is unsure whether these metals continued to stay bound due to a lack of UV-Vis peaks around 450 nm after spectroscopy analysis. Overall, experimental studies show success in creating viable energy when subjecting the nickel metalloenzymes to metal induction and photocatalysis.

Item Type: Thesis (Undergraduate)
Creators: Wills, Emory Elizabeth
Student's Degree Program(s): B.E. in Engineering
Thesis Advisor: Saumen Chakraborty
Thesis Advisor's Department: Chemistry & Biochemistry
Institution: University of Mississippi
Subjects: Q Science > QD Chemistry
Depositing User: Emory Wills
Date Deposited: 16 May 2019 19:47
Last Modified: 16 May 2019 19:51
URI: http://thesis.honors.olemiss.edu/id/eprint/1552

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