Article
Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli.
Biochemistry - 29 Mar 2011
Jha Vikash, Louis Sherif, Chelikani Prashen, Carpena Xavi, Donald Lynda J, Fita Ignacio, Loewen Peter C
Abstract excerpt
Heme-containing catalases have been extensively studied, revealing the roles of many residues, the existence of two heme orientations, flipped 180° relative to one another along the propionate-vinyl axis, and the presence of both heme b and heme d. The focus of this report is a residue, situated adjacent to the vinyl groups of the heme at the entrance of the lateral channel, with an unusual main chain geometry...
Topics
- Biocatalysis
- Catalase
- Escherichia coli
- Heme
- Isoleucine
- Models, Molecular
- Mutation
- Protein Binding
- Protein Conformation
- X-Rays