Proton NMR study of the influence on iron oxidation/ligation/spin state on the heme orientational preference in myoglobin
Proton nuclear magnetic resonance spectroscopy has been utilized to demonstrate that the degree of heme orientational disorder within a given myoglobin protein matrix can be a sensitive function of the oxidation/ligation/spin state of the heme iron. For sperm whale deuterohemin-reconstituted myoglob...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1989-01, Vol.158 (2), p.462-468 |
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| container_end_page | 468 |
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| container_title | Biochemical and biophysical research communications |
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| creator | La Mar, Gerd N. Smith, Wanda S. Davis, Nicolette L. Budd, David L. Levy, Mark J. |
| description | Proton nuclear magnetic resonance spectroscopy has been utilized to demonstrate that the degree of heme orientational disorder within a given myoglobin protein matrix can be a sensitive function of the oxidation/ligation/spin state of the heme iron. For sperm whale deuterohemin-reconstituted myoglobin, the equilibrium was found to strongly favor (5.7 to 7.8 kJ/mol) the X-ray characterized heme orientation in all six-coordinate states, but with a considerable reduction in preference (to 1.6 kJ/mol) in the five-coordinate deoxy state. In native yellow fin tuna myoglobin, changes in heme orientational preferences of ∼3 kJ/mol occur even between two six-coordinate ferric states differing solely in spin states. |
| doi_str_mv | 10.1016/S0006-291X(89)80070-1 |
| format | Article |
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For sperm whale deuterohemin-reconstituted myoglobin, the equilibrium was found to strongly favor (5.7 to 7.8 kJ/mol) the X-ray characterized heme orientation in all six-coordinate states, but with a considerable reduction in preference (to 1.6 kJ/mol) in the five-coordinate deoxy state. In native yellow fin tuna myoglobin, changes in heme orientational preferences of ∼3 kJ/mol occur even between two six-coordinate ferric states differing solely in spin states.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Crystallography</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heme</subject><subject>Hemoproteins</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Metalloproteins</subject><subject>Motion</subject><subject>Myoglobin</subject><subject>Oxidation-Reduction</subject><subject>Physeter catodon</subject><subject>Proteins</subject><subject>Whales</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv3CAUhVHVKJ2m_QmRvKiqduHmYmMMq6qK-pKStupD6g4xcEmobDMBHGX-fRnPaLbZwBXnOxe4h5BzCu8oUH7xCwB43Uj6942QbwVADzV9QlYUJNQNBfaUrI7IM_I8pX8AlDIuT8lpOeNSshXZ_oghh6n6dv2zSnm22yq4Kt9i5Sc3zDgZrIrqY1nCg7c6-zBdDP5mX6SNn4pN54Xa2W5xLHX0OOUF0UO1iegwLq0KPW7DzRDWfnpBTpweEr487Gfkz6ePvy-_1FffP3-9_HBVGwY01x1jyC0Aa53kaIwwVDdOmK53xuiutabvOOOcCYmgNTrN0PWNbRu67qzk7Rl5ve-7ieFuxpTV6JPBYdAThjmpXoietRweBWlHpRDQFLDbgyaGlMrv1Cb6UcetoqB22aglG7UbvBJSLdkoWnznhwvm9Yj26DqEUfRXB10nowcX9WR8OmK8l51kfcHe7zEsU7v3GFUyfjde6yOarGzwjzzkPzlsrZU</recordid><startdate>19890101</startdate><enddate>19890101</enddate><creator>La Mar, Gerd N.</creator><creator>Smith, Wanda S.</creator><creator>Davis, Nicolette L.</creator><creator>Budd, David L.</creator><creator>Levy, Mark J.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890101</creationdate><title>Proton NMR study of the influence on iron oxidation/ligation/spin state on the heme orientational preference in myoglobin</title><author>La Mar, Gerd N. ; Smith, Wanda S. ; Davis, Nicolette L. ; Budd, David L. ; Levy, Mark J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-544e6d0043f96ecc8c1a2f8c57fcca53dc756466489e0aaefa4ef72d321b5d963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Crystallography</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heme</topic><topic>Hemoproteins</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Metalloproteins</topic><topic>Motion</topic><topic>Myoglobin</topic><topic>Oxidation-Reduction</topic><topic>Physeter catodon</topic><topic>Proteins</topic><topic>Whales</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>La Mar, Gerd N.</creatorcontrib><creatorcontrib>Smith, Wanda S.</creatorcontrib><creatorcontrib>Davis, Nicolette L.</creatorcontrib><creatorcontrib>Budd, David L.</creatorcontrib><creatorcontrib>Levy, Mark J.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>La Mar, Gerd N.</au><au>Smith, Wanda S.</au><au>Davis, Nicolette L.</au><au>Budd, David L.</au><au>Levy, Mark J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proton NMR study of the influence on iron oxidation/ligation/spin state on the heme orientational preference in myoglobin</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1989-01-01</date><risdate>1989</risdate><volume>158</volume><issue>2</issue><spage>462</spage><epage>468</epage><pages>462-468</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Proton nuclear magnetic resonance spectroscopy has been utilized to demonstrate that the degree of heme orientational disorder within a given myoglobin protein matrix can be a sensitive function of the oxidation/ligation/spin state of the heme iron. For sperm whale deuterohemin-reconstituted myoglobin, the equilibrium was found to strongly favor (5.7 to 7.8 kJ/mol) the X-ray characterized heme orientation in all six-coordinate states, but with a considerable reduction in preference (to 1.6 kJ/mol) in the five-coordinate deoxy state. In native yellow fin tuna myoglobin, changes in heme orientational preferences of ∼3 kJ/mol occur even between two six-coordinate ferric states differing solely in spin states.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2916994</pmid><doi>10.1016/S0006-291X(89)80070-1</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1989-01, Vol.158 (2), p.462-468 |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Crystallography Fundamental and applied biological sciences. Psychology Heme Hemoproteins Magnetic Resonance Spectroscopy Metalloproteins Motion Myoglobin Oxidation-Reduction Physeter catodon Proteins Whales |
| title | Proton NMR study of the influence on iron oxidation/ligation/spin state on the heme orientational preference in myoglobin |
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