Article
Mutational study of the bacterial hemoglobin distal heme pocket.
Biochemical and biophysical research communications - 14 Jan 2005
Verma Sandhya, Patel Sangeeta, Kaur Ramandeep, Chung Yeon-Tae, Duk Brian T, Dikshit Kanak L, Stark Benjamin C, Webster Dale A
Abstract excerpt
Ligand binding experiments on three mutants in the distal heme pocket of Vitreoscilla hemoglobin (GlnE7His, ProE8Ala, and GlnE7His,ProE8Ala) were used to probe the role of GlnE7 and ProE8 in the pocket's unusual structure. The oxygen dissociation constants for the wild type, E8Ala mutant, and E7H...
Topics
- Bacterial Proteins
- Binding Sites
- Carbon Monoxide
- Escherichia coli
- Heme
- Hemoglobins
- Models, Molecular
- Mutation
- Oxygen
- Protein Conformation
- Spectroscopy, Fourier Transform Infrared
- Truncated Hemoglobins