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Electron tunneling in proteins and water

Citation

Ponce, Adrian (2000) Electron tunneling in proteins and water. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/deva-c162. https://resolver.caltech.edu/CaltechTHESIS:08062014-082923705

Abstract

The subject of this thesis is electronic coupling in donor-bridge-acceptor systems. In Chapter 2, ET properties of cyanide-bridged dinuclear ruthenium complexes were investigated. The strong interaction between the mixed-valent ruthenium centers leads to intense metal-to-metal charge transfer bands (MMCT). Hush analysis of the MMCT absorption bands yields the electronic-coupling strength between the metal centers (H_(AB)) and the total reorganization energy (λ). Comparison of ET kinetics to calculated rates shows that classical ET models fail to account for the observed kinetics and nuclear tunneling must be considered.

In Chapter 3, ET rates were measured in four ruthenium-modified highpotential iron-sulfur proteins (HiPIP), which were modified at position His50, His81, His42 and His18, respectively. ET kinetics for the His50 and His81 mutants are a factor of 300 different, while the donor-acceptor separation is nearly identical. PATHWAY calculations corroborate these measurements and highlight the importance of structural detail of the intervening protein matrix.

In Chapter 4, the distance dependence of ET through water bridges was measured. Photoinduced ET measurements in aqueous glasses at 77 K show that water is a poor medium for ET. Luminescence decay and quantum yield data were analyzed in the context of a quenching model that accounts for the exponential distance dependence of ET, the distance distribution of donors and acceptors embedded in the glass and the excluded volumes generated by the finite sizes of the donors and acceptors.

In Chapter 5, the pH-dependent excited state dynamics of ruthenium-modified amino acids were measured. The [Ru(bpy)_(3)] ^(2+) chromophore was linked to amino acids via an amide linkage. Protonation of the amide oxygen effectively quenches the excited state. In addition. time-resolved and steady-state luminescence data reveal that nonradiative rates are very sensitive to the protonation state and the structure of the amino acid moiety.

Item Type:Thesis (Dissertation (Ph.D.))
Subject Keywords:Chemistry, Electron, proteins, water
Degree Grantor:California Institute of Technology
Division:Chemistry and Chemical Engineering
Major Option:Chemistry
Thesis Availability:Public (worldwide access)
Research Advisor(s):
  • Gray, Harry B. (advisor)
  • Winkler, Jay Richmond (co-advisor)
Thesis Committee:
  • Unknown, Unknown
Defense Date:10 November 1999
Record Number:CaltechTHESIS:08062014-082923705
Persistent URL:https://resolver.caltech.edu/CaltechTHESIS:08062014-082923705
DOI:10.7907/deva-c162
Default Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:8627
Collection:CaltechTHESIS
Deposited By: Dan Anguka
Deposited On:06 Aug 2014 15:54
Last Modified:09 Nov 2022 19:19

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