Observation of deuterium-labeled diacetyldeuteroporphyrin incorporated in cyanoferrimyoglobin by deuterium nuclear magnetic resonance
Sperm whale apomyoglobin was reconstituted with selectively deuterated D 6-2,4-diacetyldeuterohemin in which the 2H label was confined to the methyl groups of the acetyl moieties. A single resonance was observed in 2H NMR of the cyanoferrimyoglobin derivative, with a chemical shift 0.80 ppm downfiel...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1975-05, Vol.64 (1), p.1-6 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Oster, Oskar Neireiter, George W. Gurd, Frank R.N. |
| description | Sperm whale apomyoglobin was reconstituted with selectively deuterated D
6-2,4-diacetyldeuterohemin in which the
2H label was confined to the methyl groups of the acetyl moieties. A single resonance was observed in
2H NMR of the cyanoferrimyoglobin derivative, with a chemical shift 0.80 ppm downfield of external D
12-TMS at pH 6.7. The corresponding chemical shift of D
6-2,4-diacetyldeuterohemin-OMe as the cyanide complex in pyridine-water was 0.96 ppm downfield of external D
12-TMS. The prominent HOD peak was well separated at 4.4 ppm downfield. The line width of the porphyrin
2H resonances in both the protein and free solvent environments yields evidence of considerable rotational freedom of the -CD3 groups about their axes. |
| doi_str_mv | 10.1016/0006-291X(75)90211-9 |
| format | Article |
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6-2,4-diacetyldeuterohemin in which the
2H label was confined to the methyl groups of the acetyl moieties. A single resonance was observed in
2H NMR of the cyanoferrimyoglobin derivative, with a chemical shift 0.80 ppm downfield of external D
12-TMS at pH 6.7. The corresponding chemical shift of D
6-2,4-diacetyldeuterohemin-OMe as the cyanide complex in pyridine-water was 0.96 ppm downfield of external D
12-TMS. The prominent HOD peak was well separated at 4.4 ppm downfield. The line width of the porphyrin
2H resonances in both the protein and free solvent environments yields evidence of considerable rotational freedom of the -CD3 groups about their axes.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(75)90211-9</identifier><identifier>PMID: 1170845</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Apoproteins ; Cetacea ; Deuterium ; Ferric Compounds ; Heme - analysis ; Magnetic Resonance Spectroscopy ; Mathematics ; Myoglobin - analysis ; Nitriles</subject><ispartof>Biochemical and biophysical research communications, 1975-05, Vol.64 (1), p.1-6</ispartof><rights>1975</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-8d198886af7da8ea49d9f450c5f1b61115394a28993235a789ab23806efe81183</citedby><cites>FETCH-LOGICAL-c357t-8d198886af7da8ea49d9f450c5f1b61115394a28993235a789ab23806efe81183</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X75902119$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1170845$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oster, Oskar</creatorcontrib><creatorcontrib>Neireiter, George W.</creatorcontrib><creatorcontrib>Gurd, Frank R.N.</creatorcontrib><title>Observation of deuterium-labeled diacetyldeuteroporphyrin incorporated in cyanoferrimyoglobin by deuterium nuclear magnetic resonance</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Sperm whale apomyoglobin was reconstituted with selectively deuterated D
6-2,4-diacetyldeuterohemin in which the
2H label was confined to the methyl groups of the acetyl moieties. A single resonance was observed in
2H NMR of the cyanoferrimyoglobin derivative, with a chemical shift 0.80 ppm downfield of external D
12-TMS at pH 6.7. The corresponding chemical shift of D
6-2,4-diacetyldeuterohemin-OMe as the cyanide complex in pyridine-water was 0.96 ppm downfield of external D
12-TMS. The prominent HOD peak was well separated at 4.4 ppm downfield. The line width of the porphyrin
2H resonances in both the protein and free solvent environments yields evidence of considerable rotational freedom of the -CD3 groups about their axes.</description><subject>Animals</subject><subject>Apoproteins</subject><subject>Cetacea</subject><subject>Deuterium</subject><subject>Ferric Compounds</subject><subject>Heme - analysis</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Mathematics</subject><subject>Myoglobin - analysis</subject><subject>Nitriles</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtq3TAQhkVoSU4ub5CAV6VZuNX4Km0CJTQXCGTTQnZiLI1TFVs6keyAH6DvXZ04JLusRqP_n3-Yj7FT4N-AQ_Odc97khYSHr219LnkBkMs9tgEueV4Arz6xzZvlgB3G-JdzgKqR-2wfoOWiqjfs330XKTzjZL3LfJ8ZmicKdh7zATsayGTGoqZpGVbFb33Y_lmCdZl1Or19wCm5Uq8XdL6nEOy4-MfBd-mvW94TMzfrgTBkIz46mqzOAkXv0Gk6Zp97HCKdvNYj9vvq56_Lm_zu_vr28sddrsu6nXJhQAohGuxbg4Kwkkb2Vc113UPXAEBdygoLIWVZlDW2QmJXlII31JMAEOUR-7LmboN_milOarRR0zCgIz9HJRKrgssmGavVqIOPMVCvtuksDIsCrnb01Q6t2qFVba1e6CuZxs5e8-duJPM-tOJO-sWqUzry2VJQUVtKAIwNpCdlvP14wX_VN5gZ</recordid><startdate>19750505</startdate><enddate>19750505</enddate><creator>Oster, Oskar</creator><creator>Neireiter, George W.</creator><creator>Gurd, Frank R.N.</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>19750505</creationdate><title>Observation of deuterium-labeled diacetyldeuteroporphyrin incorporated in cyanoferrimyoglobin by deuterium nuclear magnetic resonance</title><author>Oster, Oskar ; Neireiter, George W. ; Gurd, Frank R.N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-8d198886af7da8ea49d9f450c5f1b61115394a28993235a789ab23806efe81183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Animals</topic><topic>Apoproteins</topic><topic>Cetacea</topic><topic>Deuterium</topic><topic>Ferric Compounds</topic><topic>Heme - analysis</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Mathematics</topic><topic>Myoglobin - analysis</topic><topic>Nitriles</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oster, Oskar</creatorcontrib><creatorcontrib>Neireiter, George W.</creatorcontrib><creatorcontrib>Gurd, Frank R.N.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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>Oster, Oskar</au><au>Neireiter, George W.</au><au>Gurd, Frank R.N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Observation of deuterium-labeled diacetyldeuteroporphyrin incorporated in cyanoferrimyoglobin by deuterium nuclear magnetic resonance</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1975-05-05</date><risdate>1975</risdate><volume>64</volume><issue>1</issue><spage>1</spage><epage>6</epage><pages>1-6</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Sperm whale apomyoglobin was reconstituted with selectively deuterated D
6-2,4-diacetyldeuterohemin in which the
2H label was confined to the methyl groups of the acetyl moieties. A single resonance was observed in
2H NMR of the cyanoferrimyoglobin derivative, with a chemical shift 0.80 ppm downfield of external D
12-TMS at pH 6.7. The corresponding chemical shift of D
6-2,4-diacetyldeuterohemin-OMe as the cyanide complex in pyridine-water was 0.96 ppm downfield of external D
12-TMS. The prominent HOD peak was well separated at 4.4 ppm downfield. The line width of the porphyrin
2H resonances in both the protein and free solvent environments yields evidence of considerable rotational freedom of the -CD3 groups about their axes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>1170845</pmid><doi>10.1016/0006-291X(75)90211-9</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1975-05, Vol.64 (1), p.1-6 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82912096 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Apoproteins Cetacea Deuterium Ferric Compounds Heme - analysis Magnetic Resonance Spectroscopy Mathematics Myoglobin - analysis Nitriles |
| title | Observation of deuterium-labeled diacetyldeuteroporphyrin incorporated in cyanoferrimyoglobin by deuterium nuclear magnetic resonance |
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