Oxygen-17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases
We have obtained oxygen-17 (17O) nuclear magnetic resonance (NMR) spectra of C17O ligands bound to ferrous horseradish peroxidase isozyme A, isozyme C, and ferrous chloroperoxidase, as a function of pH. Our results show that the peroxidases exist in two distinct states, the acidic and alkaline forms...
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| Veröffentlicht in: | The Journal of biological chemistry 1988-11, Vol.263 (31), p.16118-16124 |
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| container_title | The Journal of biological chemistry |
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| creator | Lee, H C Cummings, K Hall, K Hager, L P Oldfield, E |
| description | We have obtained oxygen-17 (17O) nuclear magnetic resonance (NMR) spectra of C17O ligands bound to ferrous horseradish peroxidase isozyme A, isozyme C, and ferrous chloroperoxidase, as a function of pH. Our results show that the peroxidases exist in two distinct states, the acidic and alkaline forms, which undergo reversible acid-base-induced transitions characterized by a single pK value. The two forms are characterized spectroscopically in much the same way in all three proteins, suggesting a similar structural origin for the transition process. In particular, the 17O NMR signal of the acidic form is approximately 7 ppm more shielded than that of the alkaline form, and the CO ligand in the acidic form appears to have a smaller 17O nuclear quadrupole coupling constant than that of the alkaline form. We have also obtained the pK values and exchange rates for all three peroxidases. The results indicate that a similar structural change may be involved in the transition process in all three peroxidases. |
| doi_str_mv | 10.1016/S0021-9258(18)37566-5 |
| format | Article |
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Our results show that the peroxidases exist in two distinct states, the acidic and alkaline forms, which undergo reversible acid-base-induced transitions characterized by a single pK value. The two forms are characterized spectroscopically in much the same way in all three proteins, suggesting a similar structural origin for the transition process. In particular, the 17O NMR signal of the acidic form is approximately 7 ppm more shielded than that of the alkaline form, and the CO ligand in the acidic form appears to have a smaller 17O nuclear quadrupole coupling constant than that of the alkaline form. We have also obtained the pK values and exchange rates for all three peroxidases. The results indicate that a similar structural change may be involved in the transition process in all three peroxidases.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)37566-5</identifier><identifier>PMID: 3182785</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Carbon Monoxide - metabolism ; chloride peroxidase ; Chloride Peroxidase - metabolism ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; horseradish peroxidase ; Horseradish Peroxidase - metabolism ; Isoenzymes - metabolism ; Kinetics ; Magnetic Resonance Spectroscopy - methods ; N.M.R ; Oxidoreductases ; Oxygen Isotopes ; Peroxidases - metabolism ; Protein Binding</subject><ispartof>The Journal of biological chemistry, 1988-11, Vol.263 (31), p.16118-16124</ispartof><rights>1988 © 1988 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4115-ef91f4c1a9be4d82c2284114fb8b50daf4d8757de29505a41ee3d66d47dc7c7c3</citedby><cites>FETCH-LOGICAL-c4115-ef91f4c1a9be4d82c2284114fb8b50daf4d8757de29505a41ee3d66d47dc7c7c3</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=7081768$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3182785$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, H C</creatorcontrib><creatorcontrib>Cummings, K</creatorcontrib><creatorcontrib>Hall, K</creatorcontrib><creatorcontrib>Hager, L P</creatorcontrib><creatorcontrib>Oldfield, E</creatorcontrib><title>Oxygen-17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have obtained oxygen-17 (17O) nuclear magnetic resonance (NMR) spectra of C17O ligands bound to ferrous horseradish peroxidase isozyme A, isozyme C, and ferrous chloroperoxidase, as a function of pH. Our results show that the peroxidases exist in two distinct states, the acidic and alkaline forms, which undergo reversible acid-base-induced transitions characterized by a single pK value. The two forms are characterized spectroscopically in much the same way in all three proteins, suggesting a similar structural origin for the transition process. In particular, the 17O NMR signal of the acidic form is approximately 7 ppm more shielded than that of the alkaline form, and the CO ligand in the acidic form appears to have a smaller 17O nuclear quadrupole coupling constant than that of the alkaline form. We have also obtained the pK values and exchange rates for all three peroxidases. The results indicate that a similar structural change may be involved in the transition process in all three peroxidases.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carbon Monoxide - metabolism</subject><subject>chloride peroxidase</subject><subject>Chloride Peroxidase - metabolism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>horseradish peroxidase</subject><subject>Horseradish Peroxidase - metabolism</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>N.M.R</subject><subject>Oxidoreductases</subject><subject>Oxygen Isotopes</subject><subject>Peroxidases - metabolism</subject><subject>Protein Binding</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1P3DAQQC3Uii6Un4CUA6rgEPA4ceycKoT6JSFxKEi9WY492XWVxMFOYPff42VX22Ptg6WZN2PPMyHnQK-BQnXzm1IGec24vAR5VQheVTk_IgugssgLDn8-kMUB-UROYvxL0yprOCbHBUgmJF-Qp4f1ZolDDiIbZtOhDlmvlwNOzmQBox_0YDCLI5op-Gj8mOJxmq3DmPk2Mzo0fuj94NebEYNfO6sjxs_kY6u7iGf785Q8ff_2ePczv3_48evu9j43JQDPsa2hLQ3ousHSSmYYkylRto1sOLW6TUHBhUVWc8p1CYiFrSpbCmtE2sUp-bLrOwb_PGOcVO-iwa7TA_o5KuCMizR0AvkONGmKGLBVY3C9DhsFVG11qnedautKgVTvOhVPdef7C-amR3uo2vtL-Yt9XkejuzYkXS4eMEEliEr-w1ZuuXp1AVXjvFlhr1hVpGYKKoAt9nWHYXL24jCoaBymD7CpxEzKevef974BhHueqw</recordid><startdate>19881105</startdate><enddate>19881105</enddate><creator>Lee, H C</creator><creator>Cummings, K</creator><creator>Hall, K</creator><creator>Hager, L P</creator><creator>Oldfield, E</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19881105</creationdate><title>Oxygen-17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases</title><author>Lee, H C ; Cummings, K ; Hall, K ; Hager, L P ; Oldfield, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4115-ef91f4c1a9be4d82c2284114fb8b50daf4d8757de29505a41ee3d66d47dc7c7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carbon Monoxide - metabolism</topic><topic>chloride peroxidase</topic><topic>Chloride Peroxidase - metabolism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>horseradish peroxidase</topic><topic>Horseradish Peroxidase - metabolism</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>N.M.R</topic><topic>Oxidoreductases</topic><topic>Oxygen Isotopes</topic><topic>Peroxidases - metabolism</topic><topic>Protein Binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, H C</creatorcontrib><creatorcontrib>Cummings, K</creatorcontrib><creatorcontrib>Hall, K</creatorcontrib><creatorcontrib>Hager, L P</creatorcontrib><creatorcontrib>Oldfield, E</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, H C</au><au>Cummings, K</au><au>Hall, K</au><au>Hager, L P</au><au>Oldfield, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oxygen-17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-11-05</date><risdate>1988</risdate><volume>263</volume><issue>31</issue><spage>16118</spage><epage>16124</epage><pages>16118-16124</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have obtained oxygen-17 (17O) nuclear magnetic resonance (NMR) spectra of C17O ligands bound to ferrous horseradish peroxidase isozyme A, isozyme C, and ferrous chloroperoxidase, as a function of pH. Our results show that the peroxidases exist in two distinct states, the acidic and alkaline forms, which undergo reversible acid-base-induced transitions characterized by a single pK value. The two forms are characterized spectroscopically in much the same way in all three proteins, suggesting a similar structural origin for the transition process. In particular, the 17O NMR signal of the acidic form is approximately 7 ppm more shielded than that of the alkaline form, and the CO ligand in the acidic form appears to have a smaller 17O nuclear quadrupole coupling constant than that of the alkaline form. We have also obtained the pK values and exchange rates for all three peroxidases. The results indicate that a similar structural change may be involved in the transition process in all three peroxidases.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3182785</pmid><doi>10.1016/S0021-9258(18)37566-5</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1988-11, Vol.263 (31), p.16118-16124 |
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| language | eng |
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| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Carbon Monoxide - metabolism chloride peroxidase Chloride Peroxidase - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology horseradish peroxidase Horseradish Peroxidase - metabolism Isoenzymes - metabolism Kinetics Magnetic Resonance Spectroscopy - methods N.M.R Oxidoreductases Oxygen Isotopes Peroxidases - metabolism Protein Binding |
| title | Oxygen-17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases |
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