Mapping the electronic state crossing of a tetra-coordinated d8 complex using multi-reference quantum chemical methods

Loading...
Thumbnail Image

Authors

dePolo, Gwen E.

Issue Date

2018

Type

Thesis

Language

en_US

Keywords

Research Projects

Organizational Units

Journal Issue

Alternative Title

Abstract

The metalloproteins rubredoxin and [NiFe]-hydrogenase perform important biological functions, participating in electron transfer pathways and hydrogen oxidation/reduction respectively. The active sites of both metalloproteins have several low lying electronic spin states, providing the potential to transition from one spin state to another, which is believed to be important for these proteins’ functionality. To better understand discrepancies in the active site properties as it transitions between the tetrahedral and square planar coordinations, a simplified crystal field model consisting of a d8 Ni(II) ion and four negative point charges simulating the ligands around the Ni(II) ion is studied. For comparison, a Ni-substituted rubredoxin active site model is also characterized by quantum chemical computational methods. Pseudo-Tanabe-Sugano diagrams for the square planar and tetrahedral coordinations are created. Energies of the triplet and singlet states arising from the lowest energy 3F and 1D atomic terms are calculated and analyzed as the coordination of the point charges changes from tetrahedral to square planar.

Description

The University of Nevada, Reno Libraries will promptly respond to removal requests related to content that violates intellectual property laws, data protections, or has been uploaded without creator consent. Takedown notices should be directed to our ScholarWolf team (scholarwolf@library.unr.edu) with information about the object, including its full URL and the nature of your complaint.

Citation

Publisher

License

In Copyright

Journal

Volume

Issue

PubMed ID

DOI

ISSN

EISSN