Ligand discrimination and inhibition of heme iron autooxidation by myoglobin: Site-directed mutagenesis of a synthetic gene

Globins have evolved under strong selective pressure to overcome the natural tendency of a free heme prosthetic group to bind carbon monoxide (CO) 1000-fold more tightly than atmospheric dioxygen (O$\sb2$). Without protein-directed discrimination between these ligand molecules, the basal production of CO from various catabolic processes would inhibit the reversible transport and storage of oxygen that is necessary for life. Until recently, the exact function of active site residues in globin function has relied on studies of naturally occurring hemoglobin (Hb) mutants and globins from species with divergent active site residues.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Springer, Barry Alan

Contributors dc:contributor

• Sligar, Stephen G.

• Biology, Molecular
• Chemistry, Biochemistry

Statement dc:rights

• Copyright 1989 Springer, Barry Alan

Language dc:language

eng

Identifier

AAI9011035
(UMI)AAI9011035

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20876