Structure/function correlations of binuclear non-heme iron enzymes and their de novo models
Abstract/Contents
- Abstract
- Binuclear non-heme iron enzymes are pervasive in nature and catalyze a variety of biologically important reactions, including reactions relevant to the biosynthesis of DNA, fatty acid metabolism, the protection of pathogens from oxidative stress, cell signaling, iron storage, and many others. Elucidating the structures of their diiron active sites and the contributions of these structures to reactivity can provide molecular level insight into catalysis. The near IR circular dichroism (CD), magnetic circular dichroism (MCD), and variable temperature variable field (VTVH) MCD spectroscopies form a powerful methodology that allows for detailed structural understanding of the diiron active sites in these enzymes. Presented are studies that focus on myo-inositol oxygenase, an enzyme with significance to human health, and de novo designed diiron proteins that model native enzymes.
Description
| Type of resource | text |
|---|---|
| Form | electronic; electronic resource; remote |
| Extent | 1 online resource. |
| Publication date | 2014 |
| Issuance | monographic |
| Language | English |
Creators/Contributors
| Associated with | Snyder, Rae Ana |
|---|---|
| Associated with | Stanford University, Department of Chemistry. |
| Primary advisor | Solomon, Edward I |
| Thesis advisor | Solomon, Edward I |
| Thesis advisor | Cegelski, Lynette |
| Thesis advisor | Pande, Vijay |
| Advisor | Cegelski, Lynette |
| Advisor | Pande, Vijay |
Subjects
| Genre | Theses |
|---|
Bibliographic information
| Statement of responsibility | Rae Ana Snyder. |
|---|---|
| Note | Submitted to the Department of Chemistry. |
| Thesis | Thesis (Ph.D.)--Stanford University, 2014. |
| Location | electronic resource |
Access conditions
- Copyright
- © 2014 by Rae Ana Snyder
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