Protozoan myoglobin from Paramecium caudatum : its autoxidation reaction and hemichrome formation
Native oxymyoglobin (MbO2) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE-cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbO2 used as a reference, Paramecium MbO2 wa...
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| Veröffentlicht in: | European journal of biochemistry 1990-10, Vol.193 (1), p.55-59 |
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| creator | TSUBAMOTO, Y MATSUOKA, A YUSA, K SHIKAMA, K |
| description | Native oxymyoglobin (MbO2) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE-cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbO2 used as a reference, Paramecium MbO2 was found to be much more susceptible to autoxidation over a wide range of pH (4-11) in 0.1 M buffer at 25 degrees C. Kinetic analysis has revealed that a proton-catalyzed displacement of O2- from MbO2 by an entering water molecule can play a dominant role in the autoxidation reaction of Paramecium MbO2 to metMb, as in the case of sperm whale MbO2 involving the distal histidine as its catalytic residue. At pH values higher than 9.5, however, Paramecium MbO2 was found to be oxidized to yield a hemichrome. The spontaneous formation of hemichromes is at variance with the other known myoglobins and is therefore discussed in relation to the unusual amino acid sequence of Paramecium myoglobin having a large number of deletion. |
| doi_str_mv | 10.1111/j.1432-1033.1990.tb19303.x |
| format | Article |
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It was examined for its spectral and stability properties. When compared with sperm whale MbO2 used as a reference, Paramecium MbO2 was found to be much more susceptible to autoxidation over a wide range of pH (4-11) in 0.1 M buffer at 25 degrees C. Kinetic analysis has revealed that a proton-catalyzed displacement of O2- from MbO2 by an entering water molecule can play a dominant role in the autoxidation reaction of Paramecium MbO2 to metMb, as in the case of sperm whale MbO2 involving the distal histidine as its catalytic residue. At pH values higher than 9.5, however, Paramecium MbO2 was found to be oxidized to yield a hemichrome. The spontaneous formation of hemichromes is at variance with the other known myoglobins and is therefore discussed in relation to the unusual amino acid sequence of Paramecium myoglobin having a large number of deletion.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1990.tb19303.x</identifier><identifier>PMID: 2226448</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford: Blackwell</publisher><subject>amino acid sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Heme - chemistry ; hemichrome ; Hemoproteins ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Kinetics ; Metalloproteins ; Myoglobin - chemistry ; oxidation ; Oxidation-Reduction ; oxymyoglobin ; Paramecium - physiology ; Proteins ; spectroscopy ; Spectrum Analysis ; Whales</subject><ispartof>European journal of biochemistry, 1990-10, Vol.193 (1), p.55-59</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c318t-7c6a0cdd971f59a18e0b48daff49f3ef61e81c871f9a376959bc8cfce1c48c73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19383661$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2226448$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>TSUBAMOTO, Y</creatorcontrib><creatorcontrib>MATSUOKA, A</creatorcontrib><creatorcontrib>YUSA, K</creatorcontrib><creatorcontrib>SHIKAMA, K</creatorcontrib><title>Protozoan myoglobin from Paramecium caudatum : its autoxidation reaction and hemichrome formation</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Native oxymyoglobin (MbO2) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE-cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbO2 used as a reference, Paramecium MbO2 was found to be much more susceptible to autoxidation over a wide range of pH (4-11) in 0.1 M buffer at 25 degrees C. Kinetic analysis has revealed that a proton-catalyzed displacement of O2- from MbO2 by an entering water molecule can play a dominant role in the autoxidation reaction of Paramecium MbO2 to metMb, as in the case of sperm whale MbO2 involving the distal histidine as its catalytic residue. At pH values higher than 9.5, however, Paramecium MbO2 was found to be oxidized to yield a hemichrome. The spontaneous formation of hemichromes is at variance with the other known myoglobins and is therefore discussed in relation to the unusual amino acid sequence of Paramecium myoglobin having a large number of deletion.</description><subject>amino acid sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heme - chemistry</subject><subject>hemichrome</subject><subject>Hemoproteins</subject><subject>Hydrogen-Ion Concentration</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Metalloproteins</subject><subject>Myoglobin - chemistry</subject><subject>oxidation</subject><subject>Oxidation-Reduction</subject><subject>oxymyoglobin</subject><subject>Paramecium - physiology</subject><subject>Proteins</subject><subject>spectroscopy</subject><subject>Spectrum Analysis</subject><subject>Whales</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUU1r3TAQFKUhfU3yEwqi0N7sSJYtS7mV0C8INIfcxXotNXpYVirZ8JJfX73EpMfuZRfNjAZmCPnIWc3LXO5r3oqm4kyImmvN6mXgWjBRH96Q3Sv0luwY423V6E6-I-9z3jPGpJb9KTltmka2rdoRuE1xiU8RZhoe4-8pDn6mLsVAbyFBsOjXQBHWEZZyXFG_ZArrEg--vPg402QBnw-YR3pvg8f7orbUxRSeGefkxMGU7cW2z8jdt6931z-qm1_ff15_ualQcLVUPUpgOI66567TwJVlQ6tGcK7VTlgnuVUcVUE1iF7qTg-o0KHl2CrsxRn5_PLtQ4p_VpsXE3xGO00w27hmoxjr-051_yXyrphIrQrx6oWIKeacrDMPyQdIj4Yzc-zB7M0xbHMM2xx7MFsP5lDEHzaXdQh2fJVuwRf804ZDRphcghl9_ueghRJScvEX-0SUmQ</recordid><startdate>19901005</startdate><enddate>19901005</enddate><creator>TSUBAMOTO, Y</creator><creator>MATSUOKA, A</creator><creator>YUSA, K</creator><creator>SHIKAMA, K</creator><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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19901005</creationdate><title>Protozoan myoglobin from Paramecium caudatum : its autoxidation reaction and hemichrome formation</title><author>TSUBAMOTO, Y ; MATSUOKA, A ; YUSA, K ; SHIKAMA, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c318t-7c6a0cdd971f59a18e0b48daff49f3ef61e81c871f9a376959bc8cfce1c48c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>amino acid sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heme - chemistry</topic><topic>hemichrome</topic><topic>Hemoproteins</topic><topic>Hydrogen-Ion Concentration</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Metalloproteins</topic><topic>Myoglobin - chemistry</topic><topic>oxidation</topic><topic>Oxidation-Reduction</topic><topic>oxymyoglobin</topic><topic>Paramecium - physiology</topic><topic>Proteins</topic><topic>spectroscopy</topic><topic>Spectrum Analysis</topic><topic>Whales</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TSUBAMOTO, Y</creatorcontrib><creatorcontrib>MATSUOKA, A</creatorcontrib><creatorcontrib>YUSA, K</creatorcontrib><creatorcontrib>SHIKAMA, K</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>TSUBAMOTO, Y</au><au>MATSUOKA, A</au><au>YUSA, K</au><au>SHIKAMA, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protozoan myoglobin from Paramecium caudatum : its autoxidation reaction and hemichrome formation</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1990-10-05</date><risdate>1990</risdate><volume>193</volume><issue>1</issue><spage>55</spage><epage>59</epage><pages>55-59</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>Native oxymyoglobin (MbO2) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE-cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbO2 used as a reference, Paramecium MbO2 was found to be much more susceptible to autoxidation over a wide range of pH (4-11) in 0.1 M buffer at 25 degrees C. Kinetic analysis has revealed that a proton-catalyzed displacement of O2- from MbO2 by an entering water molecule can play a dominant role in the autoxidation reaction of Paramecium MbO2 to metMb, as in the case of sperm whale MbO2 involving the distal histidine as its catalytic residue. At pH values higher than 9.5, however, Paramecium MbO2 was found to be oxidized to yield a hemichrome. The spontaneous formation of hemichromes is at variance with the other known myoglobins and is therefore discussed in relation to the unusual amino acid sequence of Paramecium myoglobin having a large number of deletion.</abstract><cop>Oxford</cop><pub>Blackwell</pub><pmid>2226448</pmid><doi>10.1111/j.1432-1033.1990.tb19303.x</doi><tpages>5</tpages></addata></record> |
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| subjects | amino acid sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Fundamental and applied biological sciences. Psychology Heme - chemistry hemichrome Hemoproteins Hydrogen-Ion Concentration In Vitro Techniques Kinetics Metalloproteins Myoglobin - chemistry oxidation Oxidation-Reduction oxymyoglobin Paramecium - physiology Proteins spectroscopy Spectrum Analysis Whales |
| title | Protozoan myoglobin from Paramecium caudatum : its autoxidation reaction and hemichrome formation |
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