Characterization of Heme Orientational Disorder in a Myoglobin Reconstituted with a Trifluoromethyl-Group-Substituted Heme Cofactor
The orientation of a CF3-substituted heme in sperm whale myoglobin and L29F, H64L, L29F/H64Q, and H64Q variant proteins has been investigated using 19F NMR spectroscopy to elucidate structural factors responsible for the thermodynamic stability of the heme orientational disorder, i.e., the presence...
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| Veröffentlicht in: | Biochemistry (Easton) 2017-08, Vol.56 (34), p.4500-4508 |
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| creator | Kanai, Yuki Harada, Ayaka Shibata, Tomokazu Nishimura, Ryu Namiki, Kosuke Watanabe, Miho Nakamura, Shunpei Yumoto, Fumiaki Senda, Toshiya Suzuki, Akihiro Neya, Saburo Yamamoto, Yasuhiko |
| description | The orientation of a CF3-substituted heme in sperm whale myoglobin and L29F, H64L, L29F/H64Q, and H64Q variant proteins has been investigated using 19F NMR spectroscopy to elucidate structural factors responsible for the thermodynamic stability of the heme orientational disorder, i.e., the presence of two heme orientations differing by a 180° rotation about the 5–15 meso axis, with respect to the protein moiety. Crystal structure of the met-aquo form of the wild-type myoglobin reconstituted with 13,17-bis(2-carboxylatoethyl)-3,8-diethyl-2,12,18-trimethyl-7-trifluoromethylporphyrinatoiron(III), determined at resolution of 1.25 Å, revealed the presence of the heme orientational disorder. Alterations of the salt bridge between the heme 13-propionate and Arg45(CD3) side chains due to the mutations resulted in equilibrium constants of the heme orientational disorder ranging between 0.42 and 1.4. Thus, the heme orientational disorder is affected by the salt bridge associated with the heme 13-propionate side chain, confirming the importance of the salt bridge in the heme binding to the protein. |
| doi_str_mv | 10.1021/acs.biochem.7b00457 |
| format | Article |
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Crystal structure of the met-aquo form of the wild-type myoglobin reconstituted with 13,17-bis(2-carboxylatoethyl)-3,8-diethyl-2,12,18-trimethyl-7-trifluoromethylporphyrinatoiron(III), determined at resolution of 1.25 Å, revealed the presence of the heme orientational disorder. Alterations of the salt bridge between the heme 13-propionate and Arg45(CD3) side chains due to the mutations resulted in equilibrium constants of the heme orientational disorder ranging between 0.42 and 1.4. Thus, the heme orientational disorder is affected by the salt bridge associated with the heme 13-propionate side chain, confirming the importance of the salt bridge in the heme binding to the protein.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/acs.biochem.7b00457</identifier><identifier>PMID: 28758387</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Substitution ; Animals ; Binding Sites ; Crystallography, X-Ray ; Heme - chemistry ; Heme - metabolism ; Mutation, Missense ; Myoglobin - chemistry ; Myoglobin - genetics ; Myoglobin - metabolism ; Sperm Whale</subject><ispartof>Biochemistry (Easton), 2017-08, Vol.56 (34), p.4500-4508</ispartof><rights>Copyright © 2017 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a345t-a0fe5e008a306f14565c7b79209324680f61ebae5906d1d53336cb2c20afac6c3</citedby><cites>FETCH-LOGICAL-a345t-a0fe5e008a306f14565c7b79209324680f61ebae5906d1d53336cb2c20afac6c3</cites><orcidid>0000-0003-4951-3184</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00457$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.biochem.7b00457$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28758387$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kanai, Yuki</creatorcontrib><creatorcontrib>Harada, Ayaka</creatorcontrib><creatorcontrib>Shibata, Tomokazu</creatorcontrib><creatorcontrib>Nishimura, Ryu</creatorcontrib><creatorcontrib>Namiki, Kosuke</creatorcontrib><creatorcontrib>Watanabe, Miho</creatorcontrib><creatorcontrib>Nakamura, Shunpei</creatorcontrib><creatorcontrib>Yumoto, Fumiaki</creatorcontrib><creatorcontrib>Senda, Toshiya</creatorcontrib><creatorcontrib>Suzuki, Akihiro</creatorcontrib><creatorcontrib>Neya, Saburo</creatorcontrib><creatorcontrib>Yamamoto, Yasuhiko</creatorcontrib><title>Characterization of Heme Orientational Disorder in a Myoglobin Reconstituted with a Trifluoromethyl-Group-Substituted Heme Cofactor</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The orientation of a CF3-substituted heme in sperm whale myoglobin and L29F, H64L, L29F/H64Q, and H64Q variant proteins has been investigated using 19F NMR spectroscopy to elucidate structural factors responsible for the thermodynamic stability of the heme orientational disorder, i.e., the presence of two heme orientations differing by a 180° rotation about the 5–15 meso axis, with respect to the protein moiety. Crystal structure of the met-aquo form of the wild-type myoglobin reconstituted with 13,17-bis(2-carboxylatoethyl)-3,8-diethyl-2,12,18-trimethyl-7-trifluoromethylporphyrinatoiron(III), determined at resolution of 1.25 Å, revealed the presence of the heme orientational disorder. Alterations of the salt bridge between the heme 13-propionate and Arg45(CD3) side chains due to the mutations resulted in equilibrium constants of the heme orientational disorder ranging between 0.42 and 1.4. Thus, the heme orientational disorder is affected by the salt bridge associated with the heme 13-propionate side chain, confirming the importance of the salt bridge in the heme binding to the protein.</description><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Crystallography, X-Ray</subject><subject>Heme - chemistry</subject><subject>Heme - metabolism</subject><subject>Mutation, Missense</subject><subject>Myoglobin - chemistry</subject><subject>Myoglobin - genetics</subject><subject>Myoglobin - metabolism</subject><subject>Sperm Whale</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtu2zAQRYkiQeO4_YIChZbZyB4-JS0Lt40DuAiQx1qgqFHNQBJdkkLgbvvjoWMny65IDs-dCxxCvlBYUGB0qU1YNNaZLQ6LogEQsvhAZlQyyEVVyTMyAwCVs0rBBbkM4Sk9BRTiI7lgZSFLXhYz8m-11V6biN7-1dG6MXNdtsYBs1tvcYyvM91n321wvkWf2THT2a-9-927Jt3v0LgxRBuniG32bOM2fT942_WT827AuN33-bV30y6_n5p38LVh5brU7Pwnct7pPuDn0zknjz9_PKzW-eb2-mb1bZNrLmTMNXQoEaDUHFRHhVTSFE1RMag4E6qETlFsNMoKVEtbyTlXpmGGgU49yvA5uTru3Xn3Z8IQ68EGg32vR3RTqGnFRAWCUZlQfkSNdyF47Oqdt4P2-5pCfbBfJ_v1yX59sp9SX08FUzNg-555052A5RE4pJ_c5JPa8N-VL_ZelhU</recordid><startdate>20170829</startdate><enddate>20170829</enddate><creator>Kanai, Yuki</creator><creator>Harada, Ayaka</creator><creator>Shibata, Tomokazu</creator><creator>Nishimura, Ryu</creator><creator>Namiki, Kosuke</creator><creator>Watanabe, Miho</creator><creator>Nakamura, Shunpei</creator><creator>Yumoto, Fumiaki</creator><creator>Senda, Toshiya</creator><creator>Suzuki, Akihiro</creator><creator>Neya, Saburo</creator><creator>Yamamoto, Yasuhiko</creator><general>American Chemical Society</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><orcidid>https://orcid.org/0000-0003-4951-3184</orcidid></search><sort><creationdate>20170829</creationdate><title>Characterization of Heme Orientational Disorder in a Myoglobin Reconstituted with a Trifluoromethyl-Group-Substituted Heme Cofactor</title><author>Kanai, Yuki ; Harada, Ayaka ; Shibata, Tomokazu ; Nishimura, Ryu ; Namiki, Kosuke ; Watanabe, Miho ; Nakamura, Shunpei ; Yumoto, Fumiaki ; Senda, Toshiya ; Suzuki, Akihiro ; Neya, Saburo ; Yamamoto, Yasuhiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a345t-a0fe5e008a306f14565c7b79209324680f61ebae5906d1d53336cb2c20afac6c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Crystallography, X-Ray</topic><topic>Heme - chemistry</topic><topic>Heme - metabolism</topic><topic>Mutation, Missense</topic><topic>Myoglobin - chemistry</topic><topic>Myoglobin - genetics</topic><topic>Myoglobin - metabolism</topic><topic>Sperm Whale</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kanai, Yuki</creatorcontrib><creatorcontrib>Harada, Ayaka</creatorcontrib><creatorcontrib>Shibata, Tomokazu</creatorcontrib><creatorcontrib>Nishimura, Ryu</creatorcontrib><creatorcontrib>Namiki, Kosuke</creatorcontrib><creatorcontrib>Watanabe, Miho</creatorcontrib><creatorcontrib>Nakamura, Shunpei</creatorcontrib><creatorcontrib>Yumoto, Fumiaki</creatorcontrib><creatorcontrib>Senda, Toshiya</creatorcontrib><creatorcontrib>Suzuki, Akihiro</creatorcontrib><creatorcontrib>Neya, Saburo</creatorcontrib><creatorcontrib>Yamamoto, Yasuhiko</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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kanai, Yuki</au><au>Harada, Ayaka</au><au>Shibata, Tomokazu</au><au>Nishimura, Ryu</au><au>Namiki, Kosuke</au><au>Watanabe, Miho</au><au>Nakamura, Shunpei</au><au>Yumoto, Fumiaki</au><au>Senda, Toshiya</au><au>Suzuki, Akihiro</au><au>Neya, Saburo</au><au>Yamamoto, Yasuhiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of Heme Orientational Disorder in a Myoglobin Reconstituted with a Trifluoromethyl-Group-Substituted Heme Cofactor</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2017-08-29</date><risdate>2017</risdate><volume>56</volume><issue>34</issue><spage>4500</spage><epage>4508</epage><pages>4500-4508</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The orientation of a CF3-substituted heme in sperm whale myoglobin and L29F, H64L, L29F/H64Q, and H64Q variant proteins has been investigated using 19F NMR spectroscopy to elucidate structural factors responsible for the thermodynamic stability of the heme orientational disorder, i.e., the presence of two heme orientations differing by a 180° rotation about the 5–15 meso axis, with respect to the protein moiety. Crystal structure of the met-aquo form of the wild-type myoglobin reconstituted with 13,17-bis(2-carboxylatoethyl)-3,8-diethyl-2,12,18-trimethyl-7-trifluoromethylporphyrinatoiron(III), determined at resolution of 1.25 Å, revealed the presence of the heme orientational disorder. Alterations of the salt bridge between the heme 13-propionate and Arg45(CD3) side chains due to the mutations resulted in equilibrium constants of the heme orientational disorder ranging between 0.42 and 1.4. Thus, the heme orientational disorder is affected by the salt bridge associated with the heme 13-propionate side chain, confirming the importance of the salt bridge in the heme binding to the protein.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>28758387</pmid><doi>10.1021/acs.biochem.7b00457</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-4951-3184</orcidid></addata></record> |
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| subjects | Amino Acid Substitution Animals Binding Sites Crystallography, X-Ray Heme - chemistry Heme - metabolism Mutation, Missense Myoglobin - chemistry Myoglobin - genetics Myoglobin - metabolism Sperm Whale |
| title | Characterization of Heme Orientational Disorder in a Myoglobin Reconstituted with a Trifluoromethyl-Group-Substituted Heme Cofactor |
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