The F(430) cofactor of methyl coenzyme M reductase: Ligand binding to the nickel and chemical modification of the tetrapyrrole substituents

Chemical and spectroscopic studies on the nickel enzyme methyl-CoM reductase from M. thermoautotrophicum (strain $\Delta$H) were undertaken to better characterize the nickel site. The major goals of this work are two-fold: (1) To further characterize the molecular and electronic structure of the methyl-CoM reductase nickel cofactor F$\sb{430}$ as isolated and in the holoenzyme; (2) To probe the possible roles of the F$\sb{430}$ cofactor in the methyl-CoM reductase-catalyzed reduction of CH$\sb3$SCoM to CH$\sb4$. In addition, the electronic and magnetic properties of the nickel, and the iron-sulfur centers in the different redox states of methyl viologen-reducing hydrogenase from the same bacterium were investigated.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Hamilton, Cristi Lynn

• Chemistry, Analytical
• Chemistry, Inorganic
• Biophysics, General

Statement dc:rights

• Copyright 1990 Hamilton, Cristi Lynn

Language dc:language

eng

Identifier

AAI9021693
(UMI)AAI9021693

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/22068