University of Illinois at Urbana-Champaign
Molecular specificity of substrate recognition and activation in cytochrome P-450(CAM)
Abstract
dc:descriptionThe mechanisms by which biological macromolecules recognize small molecules are of fundamental relevance to the maintenance of living systems and the chemistry of noncovalent bonding. Hydrogen bonding and hydrophobic interactions have been implicated in binding and activation of hydrocarbon substrates by cytochrome P-450$\sb{\rm cam}$. The dependence of the reaction efficiency and specificity on the structural complementarity in the P-450$\sb{\rm cam}$-substrate complex suggests that the active site structure is of paramount importance in mediating catalysis. Cytochrome P-450$\sb{\rm cam}$ was used as a model system to elucidate the role of specific active site residues in substrate recognition and to engineer enzyme-substrate interactions for novel specificities.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Chemistry, Biochemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2011
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Loida, Paul John
- Contributors dc:contributor
-
- Sligar, Stephen G.
Subjects
dc:subject × 2Rights
dc:rights- Statement dc:rights
-
- Copyright 1994 Loida, Paul John
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
-
AAI9512467
(UMI)AAI9512467 - OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/23846