An effective solution for the mass production of hydrogen gas may be possible through the manipulation of hydrogenases. These metalloenzymes reversibly catalyze the evolution of molecular hydrogen from protons and electrons (2H + + 2e− ↔ H2). The active site of [Fe-Fe] hydrogenases contains a unique diiron cofactor coordinated by carbon monoxide and cyanide ligands and a dithiolate bridge. IR spectroscopy has been used here to further explore the biosynthesis, function and inhibition of this active site. For experiments observing reactions between hydrogenase samples and various reagents, a Stopped-Flow apparatus was used to ensure proper rapid mixing, and time-resolved spectra were obtained to view the transition between states with an accurate time resolution. Samples of hydrogenase from both bacterial and algal origin were studied to characterize the reduced and oxidized active states of the enzyme that are closely linked to catalytic activity. Hydrogenases were exposed to carbon monoxide to study the inhibition of the enzyme and observe changes to the active site structure. One of the first spectrums of the activated HydF maturase is presented, which may provide insight into the assembly of the H-cluster active site. And finally, IR spectra of hydrogenase samples containing different carbon and nitrogen isotopes have identified the origin of the active site ligands.
|Advisor:||Cramer, Stephen P.|
|Commitee:||Parikh, Atul, Yeh, Yin|
|School:||University of California, Davis|
|Department:||Applied Science Engineering|
|School Location:||United States -- California|
|Source:||MAI 49/02M, Masters Abstracts International|
|Subjects:||Biochemistry, Inorganic chemistry|
|Keywords:||Ftir, H-cluster, Hydrogenase, Metalloenzyme|
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