A Thermostable Cytochrome P450 From Sulfolobus Solfataricus
Weiss, Kara Elizabeth
This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.
Permalink
https://hdl.handle.net/2142/84795
Description
Title
A Thermostable Cytochrome P450 From Sulfolobus Solfataricus
Author(s)
Weiss, Kara Elizabeth
Issue Date
2003
Doctoral Committee Chair(s)
Sligar, Stephen G.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
"Crystallographic studies have revealed the placement of conserved key catalytic residues and solvent in the active site that are important in the P450 dioxygen scission reaction. CYP119 is found to display a mobile F-G helix and loop region that undergoes a significant conformational change upon binding of medium and large ligands and may reflect a natural motion independent of ligand binding. The CYP119 porphyrin is non-planar, with a ""ruffling"" and ""saddling"" of the porphyrin heterocycle. Additionally, the iron favors an in-plane position, which correlates with the spectroscopic data showing that CYP119 prefers the low-spin conformational state. This favoring of the low-spin state may have an effect on the catalytic properties of CYP119, for example the fast autoxidation rate of the oxyferrous enzyme. The overall protein structure was found to have a unique distribution of charge, which could potentially affect the normal electrostatic interaction with redox partners involved in electron transfer to the P450 cytochromes. The crystal structures of CYP119 indicate that increased stability may be due to a combination of increased factors involved in stabilizing secondary and tertiary structural interactions, such as aromatic stacking, increased salt link networks, short strong hydrogen bonds, and increased secondary structure due to shorter loops. These insights into local and globular protein stability should aid in the optimization of proteins for drug design and bio-organic chemical synthesis."
Use this login method if you
don't
have an
@illinois.edu
email address.
(Oops, I do have one)
IDEALS migrated to a new platform on June 23, 2022. If you created
your account prior to this date, you will have to reset your password
using the forgot-password link below.
