effect of EDTA and related chelating agents on the oxidation of methanol by the methylotrophic bacterium Methylophilus methylotrophus
The effects of EDTA and related metal‐chelating agents on the respiratory system of the methylotrophic bacterium Methylophilus methylotrophus have been investigated. EDTA completely inhibited whole cell methanol oxidase activity and concomitantly decreased the aerobic steady‐state reduction level of...
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| Veröffentlicht in: | European journal of biochemistry 1984-02, Vol.138 (3), p.611-615 |
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| container_title | European journal of biochemistry |
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| creator | Carver, M.A Humphrey, K.M Pathcett, R.A Jones, C.W |
| description | The effects of EDTA and related metal‐chelating agents on the respiratory system of the methylotrophic bacterium Methylophilus methylotrophus have been investigated. EDTA completely inhibited whole cell methanol oxidase activity and concomitantly decreased the aerobic steady‐state reduction level of cytochrome c, but only partially inhibited methanol dehydrogenase activity.
Analysis of the inhibition kinetics of EDTA and other chelating agents on methanol oxidase activity indicated that they were effective in the order CDTA < EDTA < HEDTA < EGTA < EDDA, and that they inhibited in an uncompetitive manner. Inhibition by EDTA varied as a function of the ambient cell mass in the assay, and could be partly reversed by the addition of divalent cations. EDTA had no effect on the activity of solubilised methanol dehydrogenase. These and other results indicate that EDTA binds a divalent metal ion, probably Mg2+, which is involved in the functional association of methanol dehydrogenase with the respiratory membrane.
This concept is discussed in terms of the electron transfer properties and spatial organisation of the terminal respiratory chain of M. methylotrophus. |
| doi_str_mv | 10.1111/j.1432-1033.1984.tb07958.x |
| format | Article |
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Analysis of the inhibition kinetics of EDTA and other chelating agents on methanol oxidase activity indicated that they were effective in the order CDTA < EDTA < HEDTA < EGTA < EDDA, and that they inhibited in an uncompetitive manner. Inhibition by EDTA varied as a function of the ambient cell mass in the assay, and could be partly reversed by the addition of divalent cations. EDTA had no effect on the activity of solubilised methanol dehydrogenase. These and other results indicate that EDTA binds a divalent metal ion, probably Mg2+, which is involved in the functional association of methanol dehydrogenase with the respiratory membrane.
This concept is discussed in terms of the electron transfer properties and spatial organisation of the terminal respiratory chain of M. methylotrophus.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1984.tb07958.x</identifier><identifier>PMID: 6420156</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Alcohol Oxidoreductases - antagonists & inhibitors ; Bacteriology ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Chelating Agents - pharmacology ; Edetic Acid - pharmacology ; Euryarchaeota - drug effects ; Euryarchaeota - enzymology ; food microbiology ; food processing ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Metabolism. Enzymes ; Methanol - metabolism ; Methylophilus methylotrophus ; Microbiology ; Mission oriented research ; NADH Dehydrogenase - antagonists & inhibitors ; Oxidation-Reduction - drug effects ; Oxygen Consumption - drug effects ; Physiology and metabolism</subject><ispartof>European journal of biochemistry, 1984-02, Vol.138 (3), p.611-615</ispartof><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5721-6311ce11a52215de4ac1f41b0399fd27a652b96df422400978e96bf1d9b7072f3</citedby><cites>FETCH-LOGICAL-c5721-6311ce11a52215de4ac1f41b0399fd27a652b96df422400978e96bf1d9b7072f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9701693$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6420156$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carver, M.A</creatorcontrib><creatorcontrib>Humphrey, K.M</creatorcontrib><creatorcontrib>Pathcett, R.A</creatorcontrib><creatorcontrib>Jones, C.W</creatorcontrib><title>effect of EDTA and related chelating agents on the oxidation of methanol by the methylotrophic bacterium Methylophilus methylotrophus</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The effects of EDTA and related metal‐chelating agents on the respiratory system of the methylotrophic bacterium Methylophilus methylotrophus have been investigated. EDTA completely inhibited whole cell methanol oxidase activity and concomitantly decreased the aerobic steady‐state reduction level of cytochrome c, but only partially inhibited methanol dehydrogenase activity.
Analysis of the inhibition kinetics of EDTA and other chelating agents on methanol oxidase activity indicated that they were effective in the order CDTA < EDTA < HEDTA < EGTA < EDDA, and that they inhibited in an uncompetitive manner. Inhibition by EDTA varied as a function of the ambient cell mass in the assay, and could be partly reversed by the addition of divalent cations. EDTA had no effect on the activity of solubilised methanol dehydrogenase. These and other results indicate that EDTA binds a divalent metal ion, probably Mg2+, which is involved in the functional association of methanol dehydrogenase with the respiratory membrane.
This concept is discussed in terms of the electron transfer properties and spatial organisation of the terminal respiratory chain of M. methylotrophus.</description><subject>Alcohol Oxidoreductases - antagonists & inhibitors</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Chelating Agents - pharmacology</subject><subject>Edetic Acid - pharmacology</subject><subject>Euryarchaeota - drug effects</subject><subject>Euryarchaeota - enzymology</subject><subject>food microbiology</subject><subject>food processing</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Metabolism. Enzymes</subject><subject>Methanol - metabolism</subject><subject>Methylophilus methylotrophus</subject><subject>Microbiology</subject><subject>Mission oriented research</subject><subject>NADH Dehydrogenase - antagonists & inhibitors</subject><subject>Oxidation-Reduction - drug effects</subject><subject>Oxygen Consumption - drug effects</subject><subject>Physiology and metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc2O0zAUhSMEGsrAIyAshNgl-PovMRs0DB1AGsRiZtaW49htqjQudiLaB-C9cUhUiRXCG_v6fPfcK50sew24gHTe7QpglOSAKS1AVqwYalxKXhXHR9nqLD3OVhgDy4nk4mn2LMYdxlhIUV5kF4IRDFyssl_WOWsG5B1af7q_QrpvULCdHmyDzHZ6tP0G6Y3th4h8j4atRf7YNuk_Valrb4et7n2H6tMfcapPnR-CP2xbg2ptBhvacY--zUL67cb4FzbG59kTp7toXyz3ZfZws76__pLffv_89frqNje8JJALCmAsgOaEAG8s0wYcgxpTKV1DSi04qaVoHCOEYSzLykpRO2hkXeKSOHqZvZ19D8H_GG0c1L6Nxnad7q0fo6qwTM7A_wkCragEOYHvZ9AEH2OwTh1Cu9fhpACrKSy1U1MiakpETWGpJSx1TM0vlyljvbfNuXVJJ-lvFl1HozsXdG_aeMZkiUFImrAPM_az7ezpPxZQN-uPdwIgObyaHZz2Sm9CGvJwl3agmHDOSsbob9i0vC0</recordid><startdate>198402</startdate><enddate>198402</enddate><creator>Carver, M.A</creator><creator>Humphrey, K.M</creator><creator>Pathcett, R.A</creator><creator>Jones, C.W</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><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>198402</creationdate><title>effect of EDTA and related chelating agents on the oxidation of methanol by the methylotrophic bacterium Methylophilus methylotrophus</title><author>Carver, M.A ; Humphrey, K.M ; Pathcett, R.A ; Jones, C.W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5721-6311ce11a52215de4ac1f41b0399fd27a652b96df422400978e96bf1d9b7072f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Alcohol Oxidoreductases - antagonists & inhibitors</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Chelating Agents - pharmacology</topic><topic>Edetic Acid - pharmacology</topic><topic>Euryarchaeota - drug effects</topic><topic>Euryarchaeota - enzymology</topic><topic>food microbiology</topic><topic>food processing</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Metabolism. Enzymes</topic><topic>Methanol - metabolism</topic><topic>Methylophilus methylotrophus</topic><topic>Microbiology</topic><topic>Mission oriented research</topic><topic>NADH Dehydrogenase - antagonists & inhibitors</topic><topic>Oxidation-Reduction - drug effects</topic><topic>Oxygen Consumption - drug effects</topic><topic>Physiology and metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carver, M.A</creatorcontrib><creatorcontrib>Humphrey, K.M</creatorcontrib><creatorcontrib>Pathcett, R.A</creatorcontrib><creatorcontrib>Jones, C.W</creatorcontrib><collection>AGRIS</collection><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>Carver, M.A</au><au>Humphrey, K.M</au><au>Pathcett, R.A</au><au>Jones, C.W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>effect of EDTA and related chelating agents on the oxidation of methanol by the methylotrophic bacterium Methylophilus methylotrophus</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1984-02</date><risdate>1984</risdate><volume>138</volume><issue>3</issue><spage>611</spage><epage>615</epage><pages>611-615</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The effects of EDTA and related metal‐chelating agents on the respiratory system of the methylotrophic bacterium Methylophilus methylotrophus have been investigated. EDTA completely inhibited whole cell methanol oxidase activity and concomitantly decreased the aerobic steady‐state reduction level of cytochrome c, but only partially inhibited methanol dehydrogenase activity.
Analysis of the inhibition kinetics of EDTA and other chelating agents on methanol oxidase activity indicated that they were effective in the order CDTA < EDTA < HEDTA < EGTA < EDDA, and that they inhibited in an uncompetitive manner. Inhibition by EDTA varied as a function of the ambient cell mass in the assay, and could be partly reversed by the addition of divalent cations. EDTA had no effect on the activity of solubilised methanol dehydrogenase. These and other results indicate that EDTA binds a divalent metal ion, probably Mg2+, which is involved in the functional association of methanol dehydrogenase with the respiratory membrane.
This concept is discussed in terms of the electron transfer properties and spatial organisation of the terminal respiratory chain of M. methylotrophus.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>6420156</pmid><doi>10.1111/j.1432-1033.1984.tb07958.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 1984-02, Vol.138 (3), p.611-615 |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Alcohol Oxidoreductases - antagonists & inhibitors Bacteriology Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Chelating Agents - pharmacology Edetic Acid - pharmacology Euryarchaeota - drug effects Euryarchaeota - enzymology food microbiology food processing Fundamental and applied biological sciences. Psychology Kinetics Metabolism. Enzymes Methanol - metabolism Methylophilus methylotrophus Microbiology Mission oriented research NADH Dehydrogenase - antagonists & inhibitors Oxidation-Reduction - drug effects Oxygen Consumption - drug effects Physiology and metabolism |
| title | effect of EDTA and related chelating agents on the oxidation of methanol by the methylotrophic bacterium Methylophilus methylotrophus |
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