Article
Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure.
Chembiochem : a European journal of chemical biology - 23 Sept 2013
Can Mehmet, Krucinska Jolanta, Zoppellaro Giorgio, Andersen Niels H, Wedekind Joseph E, Hersleth Hans-Petter, Andersson K Kristoffer, Bren Kara L
Abstract excerpt
Nitrosomonas europaea cytochrome c-552 (Ne c-552) variants with the same His/Met axial ligand set but with different EPR spectra have been characterized structurally, to aid understanding of how molecular structure determines heme electronic structure. Visible light absorption, Raman, and resonance Raman spectroscopy of the protein crystals was performed along with structure determination. The structures solved...
Topics
- Crystallography, X-Ray
- Cytochrome c Group
- Electron Spin Resonance Spectroscopy
- Electrons
- Escherichia coli
- Heme
- Hydrogen Bonding
- Mutation
- Nitrosomonas europaea
- Nuclear Magnetic Resonance, Biomolecular
- Protein Structure, Tertiary
- Recombinant Proteins