Determination of the functionally important heme peripheral vinyl group orientation in paramagnetic hemoprotein by 2D NMR
- 24 April 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 247 (2) , 263-267
- https://doi.org/10.1016/0014-5793(89)81349-3
Abstract
2D NMR spectroscopies have been successfully used to characterize the heme peripheral vinyl groups in paramagnetic hemoprotein in spite of the difficulties from the rapid paramagnetic relaxation and the low digital resolution of the 2D NMR map. The scalar coupling network system among the vinyl protons is clearly identified in the COSY spectra from its characteristic cross-peak pattern and the dipolar coupling connectivities of the vinyl proton resonances with other heme side-chain proton resonances not only provide the specific assignment of vinyl β-proton resonances but also allow the determination of the vinyl group orientation with respect to the heme plane.Keywords
This publication has 34 references indexed in Scilit:
- One- and two-dimensional nuclear Overhauser effect studies of the eletronic/molecular structure of the heme cavity of ferricytochrome b5Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- 2D NMR studies of paramagnetic lanthanide(III)-diethylenetriaminepentaacetate complexesJournal of Magnetic Resonance (1969), 1988
- Natural abundance 13C-NMR study of paramagnetic horse heart ferricytochrome c cyanide complex: Assignment of hyperfine shifted heme methyl carbon resonancesBiochemical and Biophysical Research Communications, 1988
- 13C-NMR study of labeled vinyl groups in paramagnetic myoglobin derivativesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of human hemoglobin α-chainsJournal of Molecular Biology, 1987
- X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolutionJournal of Molecular Biology, 1986
- NOE experiments for resonance and structure assignments of paramagnetic hemin derivativesJournal of Magnetic Resonance (1969), 1986
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Electronic structure of cyanide complexes of hemes and heme proteinsJournal of Molecular Biology, 1971