Crystal Structures of Modified Myoglobins. I. Heme Orientation and Structural Changes around Heme in Myoglobins Reconstituted with Isopemptoheme, Pemptoheme, 2-Ethyldeuteroheme, and 4-Ethyldeuteroheme
The crystal structures of sperm whale metmyoglobins reconstituted with four modified hemes, isopemptoheme, pemptoheme, 2-ethyldeuteroheme, and 4-ethyldeutero-heme, have been determined and refined at 2.2 Å resolution to R=0.217, 0.218, 0.213, and 0.222, respectively. All the crystals of these myoglo...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1986, Vol.100 (2), p.269-276 |
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| creator | MIKI, Kunio Yasuaki YUKAWA, Motomu OWATARI, Akira HATO, Yukinori HARADA, Shigeharu KAI, Yasushi KASAI, Nobutami HATA, Yasuo TANAKA, Nobuo KAKUDO, Masao KATSUBE, Yukiteru KAWABE, Kuniyasu YOSHTOA, Zen-ichi OGOSHI, Hisanobu |
| description | The crystal structures of sperm whale metmyoglobins reconstituted with four modified hemes, isopemptoheme, pemptoheme, 2-ethyldeuteroheme, and 4-ethyldeutero-heme, have been determined and refined at 2.2 Å resolution to R=0.217, 0.218, 0.213, and 0.222, respectively. All the crystals of these myoglobins are isomorphous with that of native metmyoglobin. The structural changes of the modified myoglobin from the native myoglobin were examined on difference Fourier maps; the orientation of 4-ethyldeuteroheme in the heme pocket is such that the heme is rotated by 180° about an axis through the α-γ-meso carbons, whereas the orientations of the other three hemes are the same as that of the protoheme in the native myoglobin. The changes of the structures around the heme become greater in the order of isopemptoheme, 2-ethyldeuteroheme < pemptoheme < 4-ethyldeuteroheme. The magnitudes of the changes seem to be related to the oxygen affinities of these four reconstituted myoglobins. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a121712 |
| format | Article |
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I. Heme Orientation and Structural Changes around Heme in Myoglobins Reconstituted with Isopemptoheme, Pemptoheme, 2-Ethyldeuteroheme, and 4-Ethyldeuteroheme</title><source>J-STAGE Free</source><source>MEDLINE</source><source>Oxford University Press Journals Digital Archive Legacy</source><source>Free Full-Text Journals in Chemistry</source><creator>MIKI, Kunio ; Yasuaki ; YUKAWA, Motomu ; OWATARI, Akira ; HATO, Yukinori ; HARADA, Shigeharu ; KAI, Yasushi ; KASAI, Nobutami ; HATA, Yasuo ; TANAKA, Nobuo ; KAKUDO, Masao ; KATSUBE, Yukiteru ; KAWABE, Kuniyasu ; YOSHTOA, Zen-ichi ; OGOSHI, Hisanobu</creator><creatorcontrib>MIKI, Kunio ; Yasuaki ; YUKAWA, Motomu ; OWATARI, Akira ; HATO, Yukinori ; HARADA, Shigeharu ; KAI, Yasushi ; KASAI, Nobutami ; HATA, Yasuo ; TANAKA, Nobuo ; KAKUDO, Masao ; KATSUBE, Yukiteru ; KAWABE, Kuniyasu ; YOSHTOA, Zen-ichi ; OGOSHI, Hisanobu</creatorcontrib><description>The crystal structures of sperm whale metmyoglobins reconstituted with four modified hemes, isopemptoheme, pemptoheme, 2-ethyldeuteroheme, and 4-ethyldeutero-heme, have been determined and refined at 2.2 Å resolution to R=0.217, 0.218, 0.213, and 0.222, respectively. All the crystals of these myoglobins are isomorphous with that of native metmyoglobin. The structural changes of the modified myoglobin from the native myoglobin were examined on difference Fourier maps; the orientation of 4-ethyldeuteroheme in the heme pocket is such that the heme is rotated by 180° about an axis through the α-γ-meso carbons, whereas the orientations of the other three hemes are the same as that of the protoheme in the native myoglobin. The changes of the structures around the heme become greater in the order of isopemptoheme, 2-ethyldeuteroheme < pemptoheme < 4-ethyldeuteroheme. The magnitudes of the changes seem to be related to the oxygen affinities of these four reconstituted myoglobins.</description><identifier>ISSN: 0021-924X</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a121712</identifier><identifier>PMID: 3782051</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; crystal structure ; Crystallization ; Fourier Analysis ; Heme ; Mathematics ; metmyoglobin ; Myoglobin ; Physeter catodon ; Protein Conformation ; Whales ; X-ray diffraction</subject><ispartof>Journal of biochemistry (Tokyo), 1986, Vol.100 (2), p.269-276</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3782051$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MIKI, Kunio</creatorcontrib><creatorcontrib>Yasuaki</creatorcontrib><creatorcontrib>YUKAWA, Motomu</creatorcontrib><creatorcontrib>OWATARI, Akira</creatorcontrib><creatorcontrib>HATO, Yukinori</creatorcontrib><creatorcontrib>HARADA, Shigeharu</creatorcontrib><creatorcontrib>KAI, Yasushi</creatorcontrib><creatorcontrib>KASAI, Nobutami</creatorcontrib><creatorcontrib>HATA, Yasuo</creatorcontrib><creatorcontrib>TANAKA, Nobuo</creatorcontrib><creatorcontrib>KAKUDO, Masao</creatorcontrib><creatorcontrib>KATSUBE, Yukiteru</creatorcontrib><creatorcontrib>KAWABE, Kuniyasu</creatorcontrib><creatorcontrib>YOSHTOA, Zen-ichi</creatorcontrib><creatorcontrib>OGOSHI, Hisanobu</creatorcontrib><title>Crystal Structures of Modified Myoglobins. I. Heme Orientation and Structural Changes around Heme in Myoglobins Reconstituted with Isopemptoheme, Pemptoheme, 2-Ethyldeuteroheme, and 4-Ethyldeuteroheme</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>The crystal structures of sperm whale metmyoglobins reconstituted with four modified hemes, isopemptoheme, pemptoheme, 2-ethyldeuteroheme, and 4-ethyldeutero-heme, have been determined and refined at 2.2 Å resolution to R=0.217, 0.218, 0.213, and 0.222, respectively. All the crystals of these myoglobins are isomorphous with that of native metmyoglobin. The structural changes of the modified myoglobin from the native myoglobin were examined on difference Fourier maps; the orientation of 4-ethyldeuteroheme in the heme pocket is such that the heme is rotated by 180° about an axis through the α-γ-meso carbons, whereas the orientations of the other three hemes are the same as that of the protoheme in the native myoglobin. The changes of the structures around the heme become greater in the order of isopemptoheme, 2-ethyldeuteroheme < pemptoheme < 4-ethyldeuteroheme. The magnitudes of the changes seem to be related to the oxygen affinities of these four reconstituted myoglobins.</description><subject>Animals</subject><subject>crystal structure</subject><subject>Crystallization</subject><subject>Fourier Analysis</subject><subject>Heme</subject><subject>Mathematics</subject><subject>metmyoglobin</subject><subject>Myoglobin</subject><subject>Physeter catodon</subject><subject>Protein Conformation</subject><subject>Whales</subject><subject>X-ray diffraction</subject><issn>0021-924X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u3CAUhVk0yl_7CJHYtKva8QUbhmU1ytQjTZRqkipRNhZjcIapDRPAauYN-1glySiK1EVXwDnfPRfdi9BnKHIoBD13T53zauNGb2Uf8s2qXeshl0CAA_mAjouCQCZIeXeETkLYPD8JpYfokPIJKSo4Rn-mfhei7PF19GMbR68Ddh2-dMp0Rit8uXMPvVsZG3I8z3GtB42vvNE2ymicxdKqt9KUMl1L-5AipHdjcl5wY9-l4KVunQ3RxDGm-N8mrvE8uK0ettGlz-uv-Me7O8ku4nrXK51ov9eeW5b_6B_RQZdmoD_tz1P0c3ZxM62zxdX3-fTbIjMERMyIEp2qgEghZaXYpNMFqzhtiWJKAZUCWAds1UmaNEIrVgLhhAqR5sXbsqSn6Mtr7ta7x1GH2AwmtLrvpdVuDA3nwNgEiv-CUPKSFAISeLYHx9WgVbP1ZpB-1-x3lPzs1Tch6qc3W_pfDeOUV019d98s6XJWz27rZkH_As-bq3c</recordid><startdate>1986</startdate><enddate>1986</enddate><creator>MIKI, Kunio</creator><creator>Yasuaki</creator><creator>YUKAWA, Motomu</creator><creator>OWATARI, Akira</creator><creator>HATO, Yukinori</creator><creator>HARADA, Shigeharu</creator><creator>KAI, Yasushi</creator><creator>KASAI, Nobutami</creator><creator>HATA, Yasuo</creator><creator>TANAKA, Nobuo</creator><creator>KAKUDO, Masao</creator><creator>KATSUBE, Yukiteru</creator><creator>KAWABE, Kuniyasu</creator><creator>YOSHTOA, Zen-ichi</creator><creator>OGOSHI, Hisanobu</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>1986</creationdate><title>Crystal Structures of Modified Myoglobins. I. Heme Orientation and Structural Changes around Heme in Myoglobins Reconstituted with Isopemptoheme, Pemptoheme, 2-Ethyldeuteroheme, and 4-Ethyldeuteroheme</title><author>MIKI, Kunio ; Yasuaki ; YUKAWA, Motomu ; OWATARI, Akira ; HATO, Yukinori ; HARADA, Shigeharu ; KAI, Yasushi ; KASAI, Nobutami ; HATA, Yasuo ; TANAKA, Nobuo ; KAKUDO, Masao ; KATSUBE, Yukiteru ; KAWABE, Kuniyasu ; YOSHTOA, Zen-ichi ; OGOSHI, Hisanobu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i219t-2d9fd512a9aa5d68fe06573c2d6dd13a916f16bfa33c22356412723998207c443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Animals</topic><topic>crystal structure</topic><topic>Crystallization</topic><topic>Fourier Analysis</topic><topic>Heme</topic><topic>Mathematics</topic><topic>metmyoglobin</topic><topic>Myoglobin</topic><topic>Physeter catodon</topic><topic>Protein Conformation</topic><topic>Whales</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MIKI, Kunio</creatorcontrib><creatorcontrib>Yasuaki</creatorcontrib><creatorcontrib>YUKAWA, Motomu</creatorcontrib><creatorcontrib>OWATARI, Akira</creatorcontrib><creatorcontrib>HATO, Yukinori</creatorcontrib><creatorcontrib>HARADA, Shigeharu</creatorcontrib><creatorcontrib>KAI, Yasushi</creatorcontrib><creatorcontrib>KASAI, Nobutami</creatorcontrib><creatorcontrib>HATA, Yasuo</creatorcontrib><creatorcontrib>TANAKA, Nobuo</creatorcontrib><creatorcontrib>KAKUDO, Masao</creatorcontrib><creatorcontrib>KATSUBE, Yukiteru</creatorcontrib><creatorcontrib>KAWABE, Kuniyasu</creatorcontrib><creatorcontrib>YOSHTOA, Zen-ichi</creatorcontrib><creatorcontrib>OGOSHI, Hisanobu</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MIKI, Kunio</au><au>Yasuaki</au><au>YUKAWA, Motomu</au><au>OWATARI, Akira</au><au>HATO, Yukinori</au><au>HARADA, Shigeharu</au><au>KAI, Yasushi</au><au>KASAI, Nobutami</au><au>HATA, Yasuo</au><au>TANAKA, Nobuo</au><au>KAKUDO, Masao</au><au>KATSUBE, Yukiteru</au><au>KAWABE, Kuniyasu</au><au>YOSHTOA, Zen-ichi</au><au>OGOSHI, Hisanobu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structures of Modified Myoglobins. I. Heme Orientation and Structural Changes around Heme in Myoglobins Reconstituted with Isopemptoheme, Pemptoheme, 2-Ethyldeuteroheme, and 4-Ethyldeuteroheme</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1986</date><risdate>1986</risdate><volume>100</volume><issue>2</issue><spage>269</spage><epage>276</epage><pages>269-276</pages><issn>0021-924X</issn><abstract>The crystal structures of sperm whale metmyoglobins reconstituted with four modified hemes, isopemptoheme, pemptoheme, 2-ethyldeuteroheme, and 4-ethyldeutero-heme, have been determined and refined at 2.2 Å resolution to R=0.217, 0.218, 0.213, and 0.222, respectively. All the crystals of these myoglobins are isomorphous with that of native metmyoglobin. The structural changes of the modified myoglobin from the native myoglobin were examined on difference Fourier maps; the orientation of 4-ethyldeuteroheme in the heme pocket is such that the heme is rotated by 180° about an axis through the α-γ-meso carbons, whereas the orientations of the other three hemes are the same as that of the protoheme in the native myoglobin. The changes of the structures around the heme become greater in the order of isopemptoheme, 2-ethyldeuteroheme < pemptoheme < 4-ethyldeuteroheme. The magnitudes of the changes seem to be related to the oxygen affinities of these four reconstituted myoglobins.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>3782051</pmid><doi>10.1093/oxfordjournals.jbchem.a121712</doi><tpages>8</tpages></addata></record> |
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| ispartof | Journal of biochemistry (Tokyo), 1986, Vol.100 (2), p.269-276 |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals Digital Archive Legacy; Free Full-Text Journals in Chemistry |
| subjects | Animals crystal structure Crystallization Fourier Analysis Heme Mathematics metmyoglobin Myoglobin Physeter catodon Protein Conformation Whales X-ray diffraction |
| title | Crystal Structures of Modified Myoglobins. I. Heme Orientation and Structural Changes around Heme in Myoglobins Reconstituted with Isopemptoheme, Pemptoheme, 2-Ethyldeuteroheme, and 4-Ethyldeuteroheme |
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