Haem localization in haemoproteins by spin and triplet tools
The rate constants of efficient exchange interaction (Kex) of spin‐labelled lysozyme and the triplet probes perylene, eosine and anthracene butanoic acid with the haemoproteins were measured in microsomes and in solution by electron paramagnetic resonance and by the registration of delayed annihilat...
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| Veröffentlicht in: | European journal of biochemistry 1986-05, Vol.156 (3), p.541-544 |
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| container_title | European journal of biochemistry |
| container_volume | 156 |
| creator | YUDANOVA, Yevgenia MECKLER, Vladimir FOGEL, Vitali KULIKOV, Alexander KOTELNIKOV, Alexander LIKHTENSTEIN, Gertz BERKOVICH, Mark KARYAKIN, Alexander ARCHAKOV, Alexander KAPLUN, Alexander SCHVETS, Vitali |
| description | The rate constants of efficient exchange interaction (Kex) of spin‐labelled lysozyme and the triplet probes perylene, eosine and anthracene butanoic acid with the haemoproteins were measured in microsomes and in solution by electron paramagnetic resonance and by the registration of delayed annihilation fluorescence. Constants of efficient exchange interactions with the haem groups of myoglobin, haemoglobin, cytochrome c and b5 are 3–22 × 107 M−1 s−1 in solution. The experiments with membrane‐bound cytochrome P‐450 revealed no exchange interactions with the probes located in solution or in the membrane. These results can be accounted for by the deeper incorporation of cytochrome P‐450 haem into the protein globule as compared to the other haemoprotein haems studied. |
| doi_str_mv | 10.1111/j.1432-1033.1986.tb09613.x |
| format | Article |
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Constants of efficient exchange interactions with the haem groups of myoglobin, haemoglobin, cytochrome c and b5 are 3–22 × 107 M−1 s−1 in solution. The experiments with membrane‐bound cytochrome P‐450 revealed no exchange interactions with the probes located in solution or in the membrane. These results can be accounted for by the deeper incorporation of cytochrome P‐450 haem into the protein globule as compared to the other haemoprotein haems studied.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1986.tb09613.x</identifier><identifier>PMID: 2422031</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Anthracenes ; Applied sciences ; Cytochromes - analysis ; E.S.R ; Electron Spin Resonance Spectroscopy ; Eosine Yellowish-(YS) ; Exact sciences and technology ; Fluorescent Dyes ; heme ; Heme - analysis ; Hemeproteins - analysis ; Hemoglobins - analysis ; hemoproteins ; Humans ; Kinetics ; liver ; microsomes ; Microsomes, Liver - metabolism ; Muramidase - analysis ; Other techniques and industries ; Rabbits ; Spin Labels</subject><ispartof>European journal of biochemistry, 1986-05, Vol.156 (3), p.541-544</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3451-f115a351c0ad5d7aaaaf499b0896fb81fe4be8c6d8524110160b7fe232ea06323</citedby><cites>FETCH-LOGICAL-c3451-f115a351c0ad5d7aaaaf499b0896fb81fe4be8c6d8524110160b7fe232ea06323</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8108350$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2422031$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>YUDANOVA, Yevgenia</creatorcontrib><creatorcontrib>MECKLER, Vladimir</creatorcontrib><creatorcontrib>FOGEL, Vitali</creatorcontrib><creatorcontrib>KULIKOV, Alexander</creatorcontrib><creatorcontrib>KOTELNIKOV, Alexander</creatorcontrib><creatorcontrib>LIKHTENSTEIN, Gertz</creatorcontrib><creatorcontrib>BERKOVICH, Mark</creatorcontrib><creatorcontrib>KARYAKIN, Alexander</creatorcontrib><creatorcontrib>ARCHAKOV, Alexander</creatorcontrib><creatorcontrib>KAPLUN, Alexander</creatorcontrib><creatorcontrib>SCHVETS, Vitali</creatorcontrib><title>Haem localization in haemoproteins by spin and triplet tools</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The rate constants of efficient exchange interaction (Kex) of spin‐labelled lysozyme and the triplet probes perylene, eosine and anthracene butanoic acid with the haemoproteins were measured in microsomes and in solution by electron paramagnetic resonance and by the registration of delayed annihilation fluorescence. Constants of efficient exchange interactions with the haem groups of myoglobin, haemoglobin, cytochrome c and b5 are 3–22 × 107 M−1 s−1 in solution. The experiments with membrane‐bound cytochrome P‐450 revealed no exchange interactions with the probes located in solution or in the membrane. These results can be accounted for by the deeper incorporation of cytochrome P‐450 haem into the protein globule as compared to the other haemoprotein haems studied.</description><subject>Animals</subject><subject>Anthracenes</subject><subject>Applied sciences</subject><subject>Cytochromes - analysis</subject><subject>E.S.R</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Eosine Yellowish-(YS)</subject><subject>Exact sciences and technology</subject><subject>Fluorescent Dyes</subject><subject>heme</subject><subject>Heme - analysis</subject><subject>Hemeproteins - analysis</subject><subject>Hemoglobins - analysis</subject><subject>hemoproteins</subject><subject>Humans</subject><subject>Kinetics</subject><subject>liver</subject><subject>microsomes</subject><subject>Microsomes, Liver - metabolism</subject><subject>Muramidase - analysis</subject><subject>Other techniques and industries</subject><subject>Rabbits</subject><subject>Spin Labels</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE1LxDAQhoMoun78BKGIeGudSdK0EUF0UVdY8KCeQ9qmmKUfa9PFXX-9KVv2Ks4lMO8zyeQh5AIhQl_Xiwg5oyECYxHKVER9BlIgi9Z7ZLKL9skEAHlIZSyOyLFzCwAQUiSH5JBySoHhhNzOtKmDqs11ZX90b9smsE3w6Zvtsmt7YxsXZJvALX1XN0XQd3ZZmT7o27Zyp-Sg1JUzZ-N5Qj6eHt-ns3D--vwyvZ-HOeMxhiVirFmMOegiLhLtq-RSZpBKUWYploZnJs1FkcaUIwIKyJLSUEaNBsEoOyFX23v9Sl8r43pVW5ebqtKNaVdOJSKR0v_sTxC5YAlLB_BmC-Zd61xnSrXsbK27jUJQg2O1UININYhUg2M1OlZrP3w-vrLKalPsRkepPr8cc-2817LTTW7dDksRUhaDx-622LetzOYfC6inx4e3mCP7BREumAg</recordid><startdate>19860502</startdate><enddate>19860502</enddate><creator>YUDANOVA, Yevgenia</creator><creator>MECKLER, Vladimir</creator><creator>FOGEL, Vitali</creator><creator>KULIKOV, Alexander</creator><creator>KOTELNIKOV, Alexander</creator><creator>LIKHTENSTEIN, Gertz</creator><creator>BERKOVICH, Mark</creator><creator>KARYAKIN, Alexander</creator><creator>ARCHAKOV, Alexander</creator><creator>KAPLUN, Alexander</creator><creator>SCHVETS, Vitali</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>C1K</scope><scope>7X8</scope></search><sort><creationdate>19860502</creationdate><title>Haem localization in haemoproteins by spin and triplet tools</title><author>YUDANOVA, Yevgenia ; MECKLER, Vladimir ; FOGEL, Vitali ; KULIKOV, Alexander ; KOTELNIKOV, Alexander ; LIKHTENSTEIN, Gertz ; BERKOVICH, Mark ; KARYAKIN, Alexander ; ARCHAKOV, Alexander ; KAPLUN, Alexander ; SCHVETS, Vitali</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3451-f115a351c0ad5d7aaaaf499b0896fb81fe4be8c6d8524110160b7fe232ea06323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Animals</topic><topic>Anthracenes</topic><topic>Applied sciences</topic><topic>Cytochromes - analysis</topic><topic>E.S.R</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Eosine Yellowish-(YS)</topic><topic>Exact sciences and technology</topic><topic>Fluorescent Dyes</topic><topic>heme</topic><topic>Heme - analysis</topic><topic>Hemeproteins - analysis</topic><topic>Hemoglobins - analysis</topic><topic>hemoproteins</topic><topic>Humans</topic><topic>Kinetics</topic><topic>liver</topic><topic>microsomes</topic><topic>Microsomes, Liver - metabolism</topic><topic>Muramidase - analysis</topic><topic>Other techniques and industries</topic><topic>Rabbits</topic><topic>Spin Labels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>YUDANOVA, Yevgenia</creatorcontrib><creatorcontrib>MECKLER, Vladimir</creatorcontrib><creatorcontrib>FOGEL, Vitali</creatorcontrib><creatorcontrib>KULIKOV, Alexander</creatorcontrib><creatorcontrib>KOTELNIKOV, Alexander</creatorcontrib><creatorcontrib>LIKHTENSTEIN, Gertz</creatorcontrib><creatorcontrib>BERKOVICH, Mark</creatorcontrib><creatorcontrib>KARYAKIN, Alexander</creatorcontrib><creatorcontrib>ARCHAKOV, Alexander</creatorcontrib><creatorcontrib>KAPLUN, Alexander</creatorcontrib><creatorcontrib>SCHVETS, Vitali</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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>YUDANOVA, Yevgenia</au><au>MECKLER, Vladimir</au><au>FOGEL, Vitali</au><au>KULIKOV, Alexander</au><au>KOTELNIKOV, Alexander</au><au>LIKHTENSTEIN, Gertz</au><au>BERKOVICH, Mark</au><au>KARYAKIN, Alexander</au><au>ARCHAKOV, Alexander</au><au>KAPLUN, Alexander</au><au>SCHVETS, Vitali</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Haem localization in haemoproteins by spin and triplet tools</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1986-05-02</date><risdate>1986</risdate><volume>156</volume><issue>3</issue><spage>541</spage><epage>544</epage><pages>541-544</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The rate constants of efficient exchange interaction (Kex) of spin‐labelled lysozyme and the triplet probes perylene, eosine and anthracene butanoic acid with the haemoproteins were measured in microsomes and in solution by electron paramagnetic resonance and by the registration of delayed annihilation fluorescence. Constants of efficient exchange interactions with the haem groups of myoglobin, haemoglobin, cytochrome c and b5 are 3–22 × 107 M−1 s−1 in solution. The experiments with membrane‐bound cytochrome P‐450 revealed no exchange interactions with the probes located in solution or in the membrane. These results can be accounted for by the deeper incorporation of cytochrome P‐450 haem into the protein globule as compared to the other haemoprotein haems studied.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2422031</pmid><doi>10.1111/j.1432-1033.1986.tb09613.x</doi><tpages>4</tpages></addata></record> |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals Anthracenes Applied sciences Cytochromes - analysis E.S.R Electron Spin Resonance Spectroscopy Eosine Yellowish-(YS) Exact sciences and technology Fluorescent Dyes heme Heme - analysis Hemeproteins - analysis Hemoglobins - analysis hemoproteins Humans Kinetics liver microsomes Microsomes, Liver - metabolism Muramidase - analysis Other techniques and industries Rabbits Spin Labels |
| title | Haem localization in haemoproteins by spin and triplet tools |
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