Article
A spectroscopic analysis of the Pro35----Ala mutant of Rhodobacter capsulatus cytochrome c2. The strictly conserved Pro35 is not structurally essential.
European journal of biochemistry - 28 Mar 1991
Gooley P R, Caffrey M S, Cusanovich M A, Mackenzie N E
Abstract excerpt
Visible, near-ultraviolet circular dichroic, near-infrared and nuclear magnetic resonance spectroscopies show that the secondary and tertiary structures of the mutant Pro35----Ala Rhodobacter capsulatus ferrocytochrome c2 are similar to the wild-type protein. The near-infrared spectrum shows that the methionine-S--Fe-heme bond is intact; however, a small red shift in the heme M transition of the near-ultraviolet...
Topics
- Circular Dichroism
- Cytochrome c Group
- Cytochromes c2
- Heme
- Magnetic Resonance Spectroscopy
- Mutation
- Protein Conformation
- Rhodobacter capsulatus
- Structure-Activity Relationship