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Evidence for a monooxygenase-catalyzed primary process in the catabolism of chlorophyll
Only recently have products of the enzymatic breakdown of the chlorophylls been characterized for the first time. All catabolites isolated until now from a chlorophyte and from angiosperms have in common the position at which the primary oxygenative ring cleavage occurs, yielding linear tetrapyrrole...
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| Published in: | FEBS letters 1995-05, Vol.364 (1), p.41-44 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c486D-3540e6ee3595686af6f59422d91d766810180b727ba22735fea8e2287c4d3333 |
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| cites | cdi_FETCH-LOGICAL-c486D-3540e6ee3595686af6f59422d91d766810180b727ba22735fea8e2287c4d3333 |
| container_end_page | 44 |
| container_issue | 1 |
| container_start_page | 41 |
| container_title | FEBS letters |
| container_volume | 364 |
| creator | Curty, Christophe Engel, Norbert Gossauer, Albert |
| description | Only recently have products of the enzymatic breakdown of the chlorophylls been characterized for the first time. All catabolites isolated until now from a chlorophyte and from angiosperms have in common the position at which the primary oxygenative ring cleavage occurs, yielding linear tetrapyrroles (19-formyl-1[21H,22H]bilinones). In vivo studies of
18,18O
2 incorporation in one of the chlorophyll catabolites isolated from
Chlorella protothecoides show unequivocally that of the two oxygen atoms inserted into the pigment, only the formyl oxygen originates from dioxygen whereas the other one, the lactamic oxygen atom, derives from water. These findings suggest a monooxygenase-catalyzed primary process in the catabolism of chlorophyll. |
| doi_str_mv | 10.1016/0014-5793(95)00348-D |
| format | article |
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18,18O
2 incorporation in one of the chlorophyll catabolites isolated from
Chlorella protothecoides show unequivocally that of the two oxygen atoms inserted into the pigment, only the formyl oxygen originates from dioxygen whereas the other one, the lactamic oxygen atom, derives from water. These findings suggest a monooxygenase-catalyzed primary process in the catabolism of chlorophyll.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)00348-D</identifier><identifier>PMID: 7750540</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>18O labeling ; 19-Formyl-1[21H,22H]bilinone ; Chlorella - enzymology ; Chlorella protothecoides ; Chlorophyll - analogs & derivatives ; Chlorophyll - metabolism ; Chlorophyll catabolism ; Mass Spectrometry ; Models, Biological ; Monooxygenase ; Oxygen - metabolism ; Oxygenases - metabolism</subject><ispartof>FEBS letters, 1995-05, Vol.364 (1), p.41-44</ispartof><rights>1995</rights><rights>FEBS Letters 364 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c486D-3540e6ee3595686af6f59422d91d766810180b727ba22735fea8e2287c4d3333</citedby><cites>FETCH-LOGICAL-c486D-3540e6ee3595686af6f59422d91d766810180b727ba22735fea8e2287c4d3333</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/001457939500348D$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3547,27922,27923,45778</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7750540$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Curty, Christophe</creatorcontrib><creatorcontrib>Engel, Norbert</creatorcontrib><creatorcontrib>Gossauer, Albert</creatorcontrib><title>Evidence for a monooxygenase-catalyzed primary process in the catabolism of chlorophyll</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Only recently have products of the enzymatic breakdown of the chlorophylls been characterized for the first time. All catabolites isolated until now from a chlorophyte and from angiosperms have in common the position at which the primary oxygenative ring cleavage occurs, yielding linear tetrapyrroles (19-formyl-1[21H,22H]bilinones). In vivo studies of
18,18O
2 incorporation in one of the chlorophyll catabolites isolated from
Chlorella protothecoides show unequivocally that of the two oxygen atoms inserted into the pigment, only the formyl oxygen originates from dioxygen whereas the other one, the lactamic oxygen atom, derives from water. These findings suggest a monooxygenase-catalyzed primary process in the catabolism of chlorophyll.</description><subject>18O labeling</subject><subject>19-Formyl-1[21H,22H]bilinone</subject><subject>Chlorella - enzymology</subject><subject>Chlorella protothecoides</subject><subject>Chlorophyll - analogs & derivatives</subject><subject>Chlorophyll - metabolism</subject><subject>Chlorophyll catabolism</subject><subject>Mass Spectrometry</subject><subject>Models, Biological</subject><subject>Monooxygenase</subject><subject>Oxygen - metabolism</subject><subject>Oxygenases - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNqNUclOwzAQtRAIyvIHIPmE4BCwk3jJBQm6ABISFySOlutMqJETl7gthK_HoVWPCF9Gnrd45hmhU0quKKH8mhCaJ0wU2UXBLgnJcpmMdtCASpElWc7lLhpsKQfoMIR3Eu-SFvtoXwhGWE4G6HW8siU0BnDlW6xx7Rvvv7o3aHSAxOiFdt03lHje2lq3XazeQAjYNngxA9wTpt7ZUGNfYTNzvvXzWefcMdqrtAtwsqlH6GUyfhk-JE_P94_D26fE5JKPkiwOARwgYwXjkuuKV6zI07QsaCk4l3FRSaYiFVOdpiJjFWgJaSqFycssniN0vraNc30sISxUbYMB53QDfhmUiFIhJY3EfE00rQ-hhUptNlKUqD5O1Wel-qxUwdRvnGoUZWcb_-W0hnIr2uQX8cka_7QOun95qsn4Lu2Bvl-w327_0M3aCGJYKwutCsb2_1LaFsxCld7-PekPsaaXXQ</recordid><startdate>19950501</startdate><enddate>19950501</enddate><creator>Curty, Christophe</creator><creator>Engel, Norbert</creator><creator>Gossauer, Albert</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>19950501</creationdate><title>Evidence for a monooxygenase-catalyzed primary process in the catabolism of chlorophyll</title><author>Curty, Christophe ; Engel, Norbert ; Gossauer, Albert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c486D-3540e6ee3595686af6f59422d91d766810180b727ba22735fea8e2287c4d3333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>18O labeling</topic><topic>19-Formyl-1[21H,22H]bilinone</topic><topic>Chlorella - enzymology</topic><topic>Chlorella protothecoides</topic><topic>Chlorophyll - analogs & derivatives</topic><topic>Chlorophyll - metabolism</topic><topic>Chlorophyll catabolism</topic><topic>Mass Spectrometry</topic><topic>Models, Biological</topic><topic>Monooxygenase</topic><topic>Oxygen - metabolism</topic><topic>Oxygenases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Curty, Christophe</creatorcontrib><creatorcontrib>Engel, Norbert</creatorcontrib><creatorcontrib>Gossauer, Albert</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Curty, Christophe</au><au>Engel, Norbert</au><au>Gossauer, Albert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for a monooxygenase-catalyzed primary process in the catabolism of chlorophyll</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-05-01</date><risdate>1995</risdate><volume>364</volume><issue>1</issue><spage>41</spage><epage>44</epage><pages>41-44</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Only recently have products of the enzymatic breakdown of the chlorophylls been characterized for the first time. All catabolites isolated until now from a chlorophyte and from angiosperms have in common the position at which the primary oxygenative ring cleavage occurs, yielding linear tetrapyrroles (19-formyl-1[21H,22H]bilinones). In vivo studies of
18,18O
2 incorporation in one of the chlorophyll catabolites isolated from
Chlorella protothecoides show unequivocally that of the two oxygen atoms inserted into the pigment, only the formyl oxygen originates from dioxygen whereas the other one, the lactamic oxygen atom, derives from water. These findings suggest a monooxygenase-catalyzed primary process in the catabolism of chlorophyll.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7750540</pmid><doi>10.1016/0014-5793(95)00348-D</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1995-05, Vol.364 (1), p.41-44 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77277881 |
| source | ScienceDirect Journals |
| subjects | 18O labeling 19-Formyl-1[21H,22H]bilinone Chlorella - enzymology Chlorella protothecoides Chlorophyll - analogs & derivatives Chlorophyll - metabolism Chlorophyll catabolism Mass Spectrometry Models, Biological Monooxygenase Oxygen - metabolism Oxygenases - metabolism |
| title | Evidence for a monooxygenase-catalyzed primary process in the catabolism of chlorophyll |
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