Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling
Reconstitution of liver fluke (Dicrocoelium dendriticum) apo-hemoglobin with hemins selectively deuterated at specific positions has permitted the assignment of several heme resonances in the proton nuclear magnetic resonance spectrum of the Met-aquo and Met-cyano forms of the holoprotein. It was es...
Published in: | Journal of Molecular Biology |
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LSU Digital Commons
1987
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Online Access: | https://digitalcommons.lsu.edu/chemistry_pubs/1977 https://doi.org/10.1016/0022-2836(87)90612-7 |
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ftlouisianastuir:oai:digitalcommons.lsu.edu:chemistry_pubs-2978 2023-06-11T04:17:07+02:00 Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling Lecomte, Juliette T.J. La Mar, Gerd N. Smit, Jan Derk G. Winterhalter, Kaspar H. Smith, Kevin M. Langry, Kevin C. Leung, Hiu Kwong 1987-09-05T07:00:00Z https://digitalcommons.lsu.edu/chemistry_pubs/1977 https://doi.org/10.1016/0022-2836(87)90612-7 unknown LSU Digital Commons https://digitalcommons.lsu.edu/chemistry_pubs/1977 doi:10.1016/0022-2836(87)90612-7 Faculty Publications text 1987 ftlouisianastuir https://doi.org/10.1016/0022-2836(87)90612-7 2023-05-28T18:15:37Z Reconstitution of liver fluke (Dicrocoelium dendriticum) apo-hemoglobin with hemins selectively deuterated at specific positions has permitted the assignment of several heme resonances in the proton nuclear magnetic resonance spectrum of the Met-aquo and Met-cyano forms of the holoprotein. It was established that in the Met-aquo form the meso protons resonate at positions characteristic of a six-co-ordinated in-plane iron. From this, we deduced that the Met-aquo species retains a bound water molecule at pH values as low as 4.5. The orientation of the proximal histidine imidazole ring with respect to the heme group in the cavity was determined through the identification of the heme methyl signals and the analysis of the hyperfine shift pattern in the Met-cyano hemoglobin proton nuclear magnetic resonance spectrum. Compared to sperm whale myoglobin, the heme appears to be rotated by 180 ° about the α, γ meso-axis. Protein isomers with the heme group in a reversed orientation were not detected, even shortly after reconstitution. In the Met-cyano form, the resonances most affected by the Bohr transition were shown to arise from the heme propionates. © 1987. Text Sperm whale LSU Digital Commons (Louisiana State University) Journal of Molecular Biology 197 1 101 110 |
institution |
Open Polar |
collection |
LSU Digital Commons (Louisiana State University) |
op_collection_id |
ftlouisianastuir |
language |
unknown |
description |
Reconstitution of liver fluke (Dicrocoelium dendriticum) apo-hemoglobin with hemins selectively deuterated at specific positions has permitted the assignment of several heme resonances in the proton nuclear magnetic resonance spectrum of the Met-aquo and Met-cyano forms of the holoprotein. It was established that in the Met-aquo form the meso protons resonate at positions characteristic of a six-co-ordinated in-plane iron. From this, we deduced that the Met-aquo species retains a bound water molecule at pH values as low as 4.5. The orientation of the proximal histidine imidazole ring with respect to the heme group in the cavity was determined through the identification of the heme methyl signals and the analysis of the hyperfine shift pattern in the Met-cyano hemoglobin proton nuclear magnetic resonance spectrum. Compared to sperm whale myoglobin, the heme appears to be rotated by 180 ° about the α, γ meso-axis. Protein isomers with the heme group in a reversed orientation were not detected, even shortly after reconstitution. In the Met-cyano form, the resonances most affected by the Bohr transition were shown to arise from the heme propionates. © 1987. |
format |
Text |
author |
Lecomte, Juliette T.J. La Mar, Gerd N. Smit, Jan Derk G. Winterhalter, Kaspar H. Smith, Kevin M. Langry, Kevin C. Leung, Hiu Kwong |
spellingShingle |
Lecomte, Juliette T.J. La Mar, Gerd N. Smit, Jan Derk G. Winterhalter, Kaspar H. Smith, Kevin M. Langry, Kevin C. Leung, Hiu Kwong Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling |
author_facet |
Lecomte, Juliette T.J. La Mar, Gerd N. Smit, Jan Derk G. Winterhalter, Kaspar H. Smith, Kevin M. Langry, Kevin C. Leung, Hiu Kwong |
author_sort |
Lecomte, Juliette T.J. |
title |
Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling |
title_short |
Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling |
title_full |
Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling |
title_fullStr |
Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling |
title_full_unstemmed |
Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: Hemin isotope labeling |
title_sort |
structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: hemin isotope labeling |
publisher |
LSU Digital Commons |
publishDate |
1987 |
url |
https://digitalcommons.lsu.edu/chemistry_pubs/1977 https://doi.org/10.1016/0022-2836(87)90612-7 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Faculty Publications |
op_relation |
https://digitalcommons.lsu.edu/chemistry_pubs/1977 doi:10.1016/0022-2836(87)90612-7 |
op_doi |
https://doi.org/10.1016/0022-2836(87)90612-7 |
container_title |
Journal of Molecular Biology |
container_volume |
197 |
container_issue |
1 |
container_start_page |
101 |
op_container_end_page |
110 |
_version_ |
1768375960275517440 |