The Role of Ergothioneine in the Oxidation of Reduced Nicotinamide Adenine Dinucleotide by Metmyoglobin or Methemoglobin
In phosphate buffer (pH 6.8), reduced nicotinamide adenine dinucleotide (NADH) was oxidized by metmyoglobin or methemoglobin in the presence of Mn (II) ion and ergothioneine. The NADH oxidation was dependent on the concentrations of Mn (II) ion, ergothioneine and metmyoglobin (or methemoglobin). Var...
Gespeichert in:
| Veröffentlicht in: | Chemical & pharmaceutical bulletin 1983/05/25, Vol.31(5), pp.1702-1707 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1707 |
|---|---|
| container_issue | 5 |
| container_start_page | 1702 |
| container_title | Chemical & pharmaceutical bulletin |
| container_volume | 31 |
| creator | MOTOHASHI, NORIKO MORI, ITSUHIKO |
| description | In phosphate buffer (pH 6.8), reduced nicotinamide adenine dinucleotide (NADH) was oxidized by metmyoglobin or methemoglobin in the presence of Mn (II) ion and ergothioneine. The NADH oxidation was dependent on the concentrations of Mn (II) ion, ergothioneine and metmyoglobin (or methemoglobin). Various phosphorus compounds also influenced the oxidation. Orthophosphate was the most effective at concentrations or more than 50 mM. In contrast, nucleotides such as adenosine-5'-triphosphate (ATP), adenosine 5'-diphosphate (ADP) and adenosine-5'-monophosphate (AMP) were less effective. Superoxide dismutase or catalase inhibited the present NADH oxidation, suggesting the participation of superoxide anion (O-2) and H2O2 in this metmyoglobin system as well as the peroxidase system. Metmyoglobin pretreated with H2O2, i.e., ferrylmyoglobin, promoted the NADH oxidation reaction, but oxymyoglobin inhibited it. A mechanism is proposed for the oxidation of NADH by metmyoglobin or methemoglobin on the basis of the redox potential of ergothioneine, the formation of Mn-phosphate complex and the heme state of metmyoglobin or methemoglobin. |
| doi_str_mv | 10.1248/cpb.31.1702 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80659217</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>80659217</sourcerecordid><originalsourceid>FETCH-LOGICAL-c635t-58e14e4a23e5f4f5918e94410d3e0033d37a645ac760bb6d7d21169d5eb5d2823</originalsourceid><addsrcrecordid>eNpdkUtr3DAUhUVpSadpVl0XDA3dFE_1sGRrGZL0AXlASNZClq5nNNjSVLIh8-8rM2YK3Ujonk_nXO5F6BPBa0Kr5rvZt2tG1qTG9A1aEVbVJaeUvUUrjLEsKRPsPfqQ0g5jynHNztCZEETUlKzQ6_MWiqfQQxG64jZuwrh1wYPzUDhfjFl8fHVWj7k4E09gJwO2eHAmjM7rwVkoriz4-cON85PpIQu52B6KexiHQ9j0oc1WIc7vLQxL4SN61-k-wcVyn6OXH7fP17_Ku8efv6-v7kojGB9L3gCpoNKUAe-qjkvSgKwqgi0DjBmzrNai4trUAretsLWlhAhpObTc0oayc_T16LuP4c8EaVSDSwb6XnsIU1INFlxSUmfwy3_gLkzR594UqbjMobIRmfp2pEwMKUXo1D66QceDIljN21B5G4oRNW8j058Xz6kdwJ7YZfxZv1x0nYzuu6i9cemESS5ZI1nGbo7YLo16Ayddx9Hlgc-RRPJmjuXHY07_J291VODZX-EYqb8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1459944986</pqid></control><display><type>article</type><title>The Role of Ergothioneine in the Oxidation of Reduced Nicotinamide Adenine Dinucleotide by Metmyoglobin or Methemoglobin</title><source>J-STAGE Free</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>MOTOHASHI, NORIKO ; MORI, ITSUHIKO</creator><creatorcontrib>MOTOHASHI, NORIKO ; MORI, ITSUHIKO</creatorcontrib><description>In phosphate buffer (pH 6.8), reduced nicotinamide adenine dinucleotide (NADH) was oxidized by metmyoglobin or methemoglobin in the presence of Mn (II) ion and ergothioneine. The NADH oxidation was dependent on the concentrations of Mn (II) ion, ergothioneine and metmyoglobin (or methemoglobin). Various phosphorus compounds also influenced the oxidation. Orthophosphate was the most effective at concentrations or more than 50 mM. In contrast, nucleotides such as adenosine-5'-triphosphate (ATP), adenosine 5'-diphosphate (ADP) and adenosine-5'-monophosphate (AMP) were less effective. Superoxide dismutase or catalase inhibited the present NADH oxidation, suggesting the participation of superoxide anion (O-2) and H2O2 in this metmyoglobin system as well as the peroxidase system. Metmyoglobin pretreated with H2O2, i.e., ferrylmyoglobin, promoted the NADH oxidation reaction, but oxymyoglobin inhibited it. A mechanism is proposed for the oxidation of NADH by metmyoglobin or methemoglobin on the basis of the redox potential of ergothioneine, the formation of Mn-phosphate complex and the heme state of metmyoglobin or methemoglobin.</description><identifier>ISSN: 0009-2363</identifier><identifier>EISSN: 1347-5223</identifier><identifier>DOI: 10.1248/cpb.31.1702</identifier><identifier>PMID: 6616721</identifier><identifier>CODEN: CPBTAL</identifier><language>eng</language><publisher>Tokyo: The Pharmaceutical Society of Japan</publisher><subject>Biological and medical sciences ; Ergothioneine - pharmacology ; General and cellular metabolism. Vitamins ; Hemeproteins - metabolism ; Medical sciences ; Methemoglobin - metabolism ; Metmyoglobin - metabolism ; NAD - metabolism ; Oxidation-Reduction ; Pharmacology. Drug treatments ; superoxide anion</subject><ispartof>Chemical and Pharmaceutical Bulletin, 1983/05/25, Vol.31(5), pp.1702-1707</ispartof><rights>The Pharmaceutical Society of Japan</rights><rights>1984 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1983</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c635t-58e14e4a23e5f4f5918e94410d3e0033d37a645ac760bb6d7d21169d5eb5d2823</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,1877,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9593893$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6616721$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MOTOHASHI, NORIKO</creatorcontrib><creatorcontrib>MORI, ITSUHIKO</creatorcontrib><title>The Role of Ergothioneine in the Oxidation of Reduced Nicotinamide Adenine Dinucleotide by Metmyoglobin or Methemoglobin</title><title>Chemical & pharmaceutical bulletin</title><addtitle>Chem. Pharm. Bull.</addtitle><description>In phosphate buffer (pH 6.8), reduced nicotinamide adenine dinucleotide (NADH) was oxidized by metmyoglobin or methemoglobin in the presence of Mn (II) ion and ergothioneine. The NADH oxidation was dependent on the concentrations of Mn (II) ion, ergothioneine and metmyoglobin (or methemoglobin). Various phosphorus compounds also influenced the oxidation. Orthophosphate was the most effective at concentrations or more than 50 mM. In contrast, nucleotides such as adenosine-5'-triphosphate (ATP), adenosine 5'-diphosphate (ADP) and adenosine-5'-monophosphate (AMP) were less effective. Superoxide dismutase or catalase inhibited the present NADH oxidation, suggesting the participation of superoxide anion (O-2) and H2O2 in this metmyoglobin system as well as the peroxidase system. Metmyoglobin pretreated with H2O2, i.e., ferrylmyoglobin, promoted the NADH oxidation reaction, but oxymyoglobin inhibited it. A mechanism is proposed for the oxidation of NADH by metmyoglobin or methemoglobin on the basis of the redox potential of ergothioneine, the formation of Mn-phosphate complex and the heme state of metmyoglobin or methemoglobin.</description><subject>Biological and medical sciences</subject><subject>Ergothioneine - pharmacology</subject><subject>General and cellular metabolism. Vitamins</subject><subject>Hemeproteins - metabolism</subject><subject>Medical sciences</subject><subject>Methemoglobin - metabolism</subject><subject>Metmyoglobin - metabolism</subject><subject>NAD - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Pharmacology. Drug treatments</subject><subject>superoxide anion</subject><issn>0009-2363</issn><issn>1347-5223</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtr3DAUhUVpSadpVl0XDA3dFE_1sGRrGZL0AXlASNZClq5nNNjSVLIh8-8rM2YK3Ujonk_nXO5F6BPBa0Kr5rvZt2tG1qTG9A1aEVbVJaeUvUUrjLEsKRPsPfqQ0g5jynHNztCZEETUlKzQ6_MWiqfQQxG64jZuwrh1wYPzUDhfjFl8fHVWj7k4E09gJwO2eHAmjM7rwVkoriz4-cON85PpIQu52B6KexiHQ9j0oc1WIc7vLQxL4SN61-k-wcVyn6OXH7fP17_Ku8efv6-v7kojGB9L3gCpoNKUAe-qjkvSgKwqgi0DjBmzrNai4trUAretsLWlhAhpObTc0oayc_T16LuP4c8EaVSDSwb6XnsIU1INFlxSUmfwy3_gLkzR594UqbjMobIRmfp2pEwMKUXo1D66QceDIljN21B5G4oRNW8j058Xz6kdwJ7YZfxZv1x0nYzuu6i9cemESS5ZI1nGbo7YLo16Ayddx9Hlgc-RRPJmjuXHY07_J291VODZX-EYqb8</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>MOTOHASHI, NORIKO</creator><creator>MORI, ITSUHIKO</creator><general>The Pharmaceutical Society of Japan</general><general>Maruzen</general><general>Japan Science and Technology Agency</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>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19830101</creationdate><title>The Role of Ergothioneine in the Oxidation of Reduced Nicotinamide Adenine Dinucleotide by Metmyoglobin or Methemoglobin</title><author>MOTOHASHI, NORIKO ; MORI, ITSUHIKO</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c635t-58e14e4a23e5f4f5918e94410d3e0033d37a645ac760bb6d7d21169d5eb5d2823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Biological and medical sciences</topic><topic>Ergothioneine - pharmacology</topic><topic>General and cellular metabolism. Vitamins</topic><topic>Hemeproteins - metabolism</topic><topic>Medical sciences</topic><topic>Methemoglobin - metabolism</topic><topic>Metmyoglobin - metabolism</topic><topic>NAD - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Pharmacology. Drug treatments</topic><topic>superoxide anion</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MOTOHASHI, NORIKO</creatorcontrib><creatorcontrib>MORI, ITSUHIKO</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>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical & pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MOTOHASHI, NORIKO</au><au>MORI, ITSUHIKO</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Role of Ergothioneine in the Oxidation of Reduced Nicotinamide Adenine Dinucleotide by Metmyoglobin or Methemoglobin</atitle><jtitle>Chemical & pharmaceutical bulletin</jtitle><addtitle>Chem. Pharm. Bull.</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>31</volume><issue>5</issue><spage>1702</spage><epage>1707</epage><pages>1702-1707</pages><issn>0009-2363</issn><eissn>1347-5223</eissn><coden>CPBTAL</coden><abstract>In phosphate buffer (pH 6.8), reduced nicotinamide adenine dinucleotide (NADH) was oxidized by metmyoglobin or methemoglobin in the presence of Mn (II) ion and ergothioneine. The NADH oxidation was dependent on the concentrations of Mn (II) ion, ergothioneine and metmyoglobin (or methemoglobin). Various phosphorus compounds also influenced the oxidation. Orthophosphate was the most effective at concentrations or more than 50 mM. In contrast, nucleotides such as adenosine-5'-triphosphate (ATP), adenosine 5'-diphosphate (ADP) and adenosine-5'-monophosphate (AMP) were less effective. Superoxide dismutase or catalase inhibited the present NADH oxidation, suggesting the participation of superoxide anion (O-2) and H2O2 in this metmyoglobin system as well as the peroxidase system. Metmyoglobin pretreated with H2O2, i.e., ferrylmyoglobin, promoted the NADH oxidation reaction, but oxymyoglobin inhibited it. A mechanism is proposed for the oxidation of NADH by metmyoglobin or methemoglobin on the basis of the redox potential of ergothioneine, the formation of Mn-phosphate complex and the heme state of metmyoglobin or methemoglobin.</abstract><cop>Tokyo</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>6616721</pmid><doi>10.1248/cpb.31.1702</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0009-2363 |
| ispartof | Chemical and Pharmaceutical Bulletin, 1983/05/25, Vol.31(5), pp.1702-1707 |
| issn | 0009-2363 1347-5223 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80659217 |
| source | J-STAGE Free; MEDLINE; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Biological and medical sciences Ergothioneine - pharmacology General and cellular metabolism. Vitamins Hemeproteins - metabolism Medical sciences Methemoglobin - metabolism Metmyoglobin - metabolism NAD - metabolism Oxidation-Reduction Pharmacology. Drug treatments superoxide anion |
| title | The Role of Ergothioneine in the Oxidation of Reduced Nicotinamide Adenine Dinucleotide by Metmyoglobin or Methemoglobin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T14%3A19%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Role%20of%20Ergothioneine%20in%20the%20Oxidation%20of%20Reduced%20Nicotinamide%20Adenine%20Dinucleotide%20by%20Metmyoglobin%20or%20Methemoglobin&rft.jtitle=Chemical%20&%20pharmaceutical%20bulletin&rft.au=MOTOHASHI,%20NORIKO&rft.date=1983-01-01&rft.volume=31&rft.issue=5&rft.spage=1702&rft.epage=1707&rft.pages=1702-1707&rft.issn=0009-2363&rft.eissn=1347-5223&rft.coden=CPBTAL&rft_id=info:doi/10.1248/cpb.31.1702&rft_dat=%3Cproquest_cross%3E80659217%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1459944986&rft_id=info:pmid/6616721&rfr_iscdi=true |