Spectroscopic characterization of heme A reconstituted myoglobin.

abstract

• 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.

authors

• Musser, Siegfried

published proceedings

• J Inorg Biochem

author list (cited authors)

• Larsen, R. W., Nunez, D. J., MacLeod, J., Shiemke, A. K., Musser, S. M., Nguyen, H. H., Ondrias, M. R., & Chan, S. I.

citation count

• 8

complete list of authors

• Larsen, RW||Nunez, DJ||MacLeod, J||Shiemke, AK||Musser, SM||Nguyen, HH||Ondrias, MR||Chan, SI

publication date

• October 1992

publisher

• Elsevier  Publisher

published in

• Journal of Inorganic Biochemistry  Journal

keywords

• Animals
• Cattle
• Dimethyl Sulfoxide
• Electron Spin Resonance Spectroscopy
• Ferric Compounds
• Ferrous Compounds
• Heme
• Myoglobin
• Protein Conformation
• Spectrum Analysis
• Spectrum Analysis, Raman
• Structure-Activity Relationship

PubMed Central ID

• 1326598

Digital Object Identifier (DOI)

• 10.1016/0162-0134(92)80049-2

start page

• 21

end page

• 31

volume

• 48

issue

• 1

URL

• http://dx.doi.org/10.1016/0162-0134(92)80049-2