Spectroscopic characterization of heme A reconstituted myoglobin
| Autor: | Andrew K. Shiemke, Jason D. MacLeod, Siegfried M. Musser, Randy W. Larsen, Mark R. Ondrias, Sunney I. Chan, David J. Nunez, Hiep Hoa Nguyen |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Hemeprotein
Stereochemistry Protein Conformation Heme Photochemistry Spectrum Analysis Raman Biochemistry Ferric Compounds law.invention Inorganic Chemistry chemistry.chemical_compound Structure-Activity Relationship Protein structure law Animals Dimethyl Sulfoxide Ferrous Compounds Electron paramagnetic resonance Chemistry Myoglobin Spectrum Analysis Electron Spin Resonance Spectroscopy Chromophore Porphyrin Heme A Cattle |
| Zdroj: | Journal of inorganic biochemistry. 48(1) |
| ISSN: | 0162-0134 |
| Popis: | The focus of this study was to examine the functional role of the unusual peripheral substitution of heme A. The effects of heme A stereochemistry on the reconstitution of the porphyrin have been examined in the heme A-apo-myoglobin complex using optical absorption and resonance Raman and electron paramagnetic resonance spectroscopies. The addition of one equivalent of heme A to apo-Mb produces a complex which displays spectroscopic signals consistent with a distribution of high- and low-spin heme chromophores. These results indicate that the incorporation of heme A into apo-Mb significantly perturbs the protein refolding. |
| Databáze: | OpenAIRE |
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