Article
Characterization of heme-coordinating histidyl residues of an engineered six-coordinated myoglobin mutant based on the reactivity with diethylpyrocarbonate, mass spectrometry, and electron paramagnetic resonance spectroscopy.
Journal of bioscience and bioengineering - 1 Jun 2008
Nakanishi Nobuyuki, Takeuchi Fusako, Park Sam-Yong, Hori Hiroshi, Kiyota Kohei, Uno Tadayuki, Tsubaki Motonari
Abstract excerpt
A genetically engineered porcine myoglobin triple mutant (H64V/V68H/H93A) (VHA-Mb) contains 6 non-axial His residues (His24, His36, His48, His81, His82, and His119) besides two candidate axial His residues (His68 and His97). Although previous resonance Raman study on the ferric VHA-Mb were not conclusive for its coordination structure, present EPR parameters of the ferric VHA-Mb were consistent with bis-imidazole...
Topics
- Diethyl Pyrocarbonate
- Electron Spin Resonance Spectroscopy
- Heme
- Histidine
- Mass Spectrometry
- Mutation
- Myoglobin
- Protein Engineering
- Protein Structure, Tertiary