Rivas Mata, Jose E.
(2024)
Electron transfer rate of Cytochrome c immobilized on chiral self-assembled monolayers.
Master's Thesis, University of Pittsburgh.
(Unpublished)
This is the latest version of this item.
Abstract
Protein film voltammetry (PFV) techniques are used to study and characterize electrochemical and physicochemical properties of redox biomolecules. One technique, consists in employing self-assembled monolayers (SAMs) with a head group that allows a redox enzyme to immobilize over the surface of an electrode, leading to non-destructive studies and a design that imitates the biological one. Cytochrome c (Cyt c) is a small protein that has been widely studied due to its importance in metabolic and respiratory cycles, and the ease in which it forms a reversible electron-transfer complex on SAMs. This work covers two sections, (1) the importance of chirality on electron transfer in biomimetic systems (2) and the effect of the electrolyte’s pH on electron transfer. A tripeptide SAM consisting of Cysteine, Alanine, and Glutamic acid, respectively, was employed for the chirality based experiments, focused on LLL, LDL, and DDD enantiomeric forms. The LLL-tripeptide demonstrated to have a higher electron transfer rate (k0) in comparison to the other enantiomers, showing that electron transfer is favored by homochirality; moreover, by breaking the homochirality, the k0 drops significantly. The spin polarization displayed by the LLL and DDD-tripeptide also cause the magnetization of ferromagnetic electrode (Ni/Au) to affect the electron transfer rate. This effect on electron transfer and the effect of homochirality correlate with the chiral induced spin selectivity (CISS) effect. In addition, pH dependence experiments were carried out by using pure 8-mercaptooctanoic acid SAM and mixed with 6-mercapto-1-hexanol. The results demonstrated that a more basic pH gives a slower k0, in relation to a more acidic one.
Share
| Citation/Export: |
|
| Social Networking: |
|
Details
| Item Type: |
University of Pittsburgh ETD
|
| Status: |
Unpublished |
| Creators/Authors: |
|
| ETD Committee: |
|
| Date: |
27 August 2024 |
| Date Type: |
Publication |
| Defense Date: |
26 April 2024 |
| Approval Date: |
27 August 2024 |
| Submission Date: |
10 July 2024 |
| Access Restriction: |
No restriction; Release the ETD for access worldwide immediately. |
| Number of Pages: |
46 |
| Institution: |
University of Pittsburgh |
| Schools and Programs: |
Dietrich School of Arts and Sciences > Chemistry |
| Degree: |
MS - Master of Science |
| Thesis Type: |
Master's Thesis |
| Refereed: |
Yes |
| Uncontrolled Keywords: |
Electrochemistry, Self-assembled monolayers, Cytochrome c, Chirality Induced Spin Selectivity Effect, Electron transfer, CISS, SAM. |
| Date Deposited: |
27 Aug 2024 13:16 |
| Last Modified: |
27 Aug 2024 13:16 |
| URI: |
http://d-scholarship.pitt.edu/id/eprint/46683 |
Available Versions of this Item
-
Electron transfer rate of Cytochrome c immobilized on chiral self-assembled monolayers. (deposited 27 Aug 2024 13:16)
[Currently Displayed]
Metrics
Monthly Views for the past 3 years
Plum Analytics
Actions (login required)
 |
View Item |
![[feed]](/images/feed-icon-32x32.png){kind=icon}