Metals in Chemistry and Biology: Computational Chemistry Studies

Numerous enzymatic reactions are controlled by the chemistry of metallic ions. This dissertation investigates the electronic properties of three transition metal (copper, chromium, and nickel) complexes and describes modeling studies performed on glutathione synthetase. (1) Copper nitrene complexes were computationally characterized, as these complexes have yet to be experimentally isolated. (2) Multireference calculations were carried out on a symmetric C2v chromium dimer derived from the crystal structure of the [(tBu3SiO)Cr(µ-OSitBu3)]2 complex. (3) The T-shaped geometry of a three-coordinate β-diketiminate nickel(I) complex with a CO ligand was compared and contrasted with isoelectronic and isosteric copper(II) complexes. (4) Glutathione synthetase (GS), an enzyme that belongs to the ATP-grasp superfamily, catalyzes the (Mg, ATP)-dependent biosynthesis of glutathione (GSH) from γ-glutamylcysteine and glycine. The free and reactant forms of human GS (wild-type and glycine mutants) were modeled computationally by employing molecular dynamics simulations, as these currently have not been structurally characterized.

Grantor dc:publisher

University of North Texas

Year dc:date

2007

Author dc:creator

• Dinescu, Adriana

Contributors dc:contributor

• Cundari, Thomas R.
• Omary, Mohammad
• Schwartz, Martin
• Wilson, Angela K.

• quantum chemistry
• density functional theory
• multireference methods
• molecular mechanics
• molecular dynamics
• Transition metals.
• Glutathione.
• Enzymes.
• Metal ions.

Statement dc:rights

• Public
• Copyright
• Dinescu, Adriana
• Copyright is held by the author, unless otherwise noted. All rights reserved.

Language dc:language

English

Identifier

oclc: 179920709
https://digital.library.unt.edu/ark:/67531/metadc3678/
ark: ark:/67531/metadc3678

OAI identifier oai:identifier

info:ark/67531/metadc3678