An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light
Chlorophyllous pigments are essential for photosynthesis. Bacteriochlorophyll (BChl) b has the characteristic C8-ethylidene group and therefore is the sole naturally occurring pigment having an absorption maximum at near-infrared light wavelength. Here we report that chlorophyllide a oxidoreductase...
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| Veröffentlicht in: | Scientific reports 2013-02, Vol.3 (1), p.1217-1217, Article 1217 |
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| creator | Tsukatani, Yusuke Yamamoto, Haruki Harada, Jiro Yoshitomi, Taichi Nomata, Jiro Kasahara, Masahiro Mizoguchi, Tadashi Fujita, Yuichi Tamiaki, Hitoshi |
| description | Chlorophyllous pigments are essential for photosynthesis. Bacteriochlorophyll (BChl)
b
has the characteristic C8-ethylidene group and therefore is the sole naturally occurring pigment having an absorption maximum at near-infrared light wavelength. Here we report that chlorophyllide
a
oxidoreductase (COR), a nitrogenase-like enzyme, showed distinct substrate recognition and catalytic reaction between BChl
a-
and
b
-producing proteobacteria. COR from BChl
b
-producing
Blastochloris viridis
synthesized the C8-ethylidene group from 8-vinyl-chlorophyllide
a
. In contrast, despite the highly conserved primary structures, COR from BChl
a
-producing
Rhodobacter capsulatus
catalyzes the C8-vinyl reduction as well as the previously known reaction of the C7 = C8 double bond reduction on 8-vinyl-chlorophyllide
a
. The present data indicate that the plasticity of the nitrogenase-like enzyme caused the branched pathways of BChls
a
and
b
biosynthesis, ultimately leading to ecologically different niches of BChl
a
- and
b
-based photosynthesis differentiated by more than 150 nm wavelength. |
| doi_str_mv | 10.1038/srep01217 |
| format | Article |
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b
has the characteristic C8-ethylidene group and therefore is the sole naturally occurring pigment having an absorption maximum at near-infrared light wavelength. Here we report that chlorophyllide
a
oxidoreductase (COR), a nitrogenase-like enzyme, showed distinct substrate recognition and catalytic reaction between BChl
a-
and
b
-producing proteobacteria. COR from BChl
b
-producing
Blastochloris viridis
synthesized the C8-ethylidene group from 8-vinyl-chlorophyllide
a
. In contrast, despite the highly conserved primary structures, COR from BChl
a
-producing
Rhodobacter capsulatus
catalyzes the C8-vinyl reduction as well as the previously known reaction of the C7 = C8 double bond reduction on 8-vinyl-chlorophyllide
a
. The present data indicate that the plasticity of the nitrogenase-like enzyme caused the branched pathways of BChls
a
and
b
biosynthesis, ultimately leading to ecologically different niches of BChl
a
- and
b
-based photosynthesis differentiated by more than 150 nm wavelength.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep01217</identifier><identifier>PMID: 23386973</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/181/735 ; 631/449/1734 ; 631/45/612/1141 ; 631/61/350 ; Alphaproteobacteria - enzymology ; Alphaproteobacteria - metabolism ; Bacteriochlorophyll A - chemistry ; Bacteriochlorophyll A - metabolism ; Bacteriochlorophylls - chemistry ; Bacteriochlorophylls - metabolism ; Biosynthetic Pathways ; Humanities and Social Sciences ; multidisciplinary ; Oxidoreductases Acting on CH-CH Group Donors - chemistry ; Oxidoreductases Acting on CH-CH Group Donors - genetics ; Oxidoreductases Acting on CH-CH Group Donors - metabolism ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Rhodobacter capsulatus - enzymology ; Rhodobacter capsulatus - metabolism ; Science ; Spectroscopy, Near-Infrared ; Substrate Specificity</subject><ispartof>Scientific reports, 2013-02, Vol.3 (1), p.1217-1217, Article 1217</ispartof><rights>The Author(s) 2013</rights><rights>Copyright © 2013, Macmillan Publishers Limited. All rights reserved 2013 Macmillan Publishers Limited. All rights reserved</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-cbd7300cc61806a85890820e2738d6b13846268438adc9d76663fde1176c6bfb3</citedby><cites>FETCH-LOGICAL-c520t-cbd7300cc61806a85890820e2738d6b13846268438adc9d76663fde1176c6bfb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3564038/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3564038/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23386973$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsukatani, Yusuke</creatorcontrib><creatorcontrib>Yamamoto, Haruki</creatorcontrib><creatorcontrib>Harada, Jiro</creatorcontrib><creatorcontrib>Yoshitomi, Taichi</creatorcontrib><creatorcontrib>Nomata, Jiro</creatorcontrib><creatorcontrib>Kasahara, Masahiro</creatorcontrib><creatorcontrib>Mizoguchi, Tadashi</creatorcontrib><creatorcontrib>Fujita, Yuichi</creatorcontrib><creatorcontrib>Tamiaki, Hitoshi</creatorcontrib><title>An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Chlorophyllous pigments are essential for photosynthesis. Bacteriochlorophyll (BChl)
b
has the characteristic C8-ethylidene group and therefore is the sole naturally occurring pigment having an absorption maximum at near-infrared light wavelength. Here we report that chlorophyllide
a
oxidoreductase (COR), a nitrogenase-like enzyme, showed distinct substrate recognition and catalytic reaction between BChl
a-
and
b
-producing proteobacteria. COR from BChl
b
-producing
Blastochloris viridis
synthesized the C8-ethylidene group from 8-vinyl-chlorophyllide
a
. In contrast, despite the highly conserved primary structures, COR from BChl
a
-producing
Rhodobacter capsulatus
catalyzes the C8-vinyl reduction as well as the previously known reaction of the C7 = C8 double bond reduction on 8-vinyl-chlorophyllide
a
. The present data indicate that the plasticity of the nitrogenase-like enzyme caused the branched pathways of BChls
a
and
b
biosynthesis, ultimately leading to ecologically different niches of BChl
a
- and
b
-based photosynthesis differentiated by more than 150 nm wavelength.</description><subject>631/181/735</subject><subject>631/449/1734</subject><subject>631/45/612/1141</subject><subject>631/61/350</subject><subject>Alphaproteobacteria - enzymology</subject><subject>Alphaproteobacteria - metabolism</subject><subject>Bacteriochlorophyll A - chemistry</subject><subject>Bacteriochlorophyll A - metabolism</subject><subject>Bacteriochlorophylls - chemistry</subject><subject>Bacteriochlorophylls - metabolism</subject><subject>Biosynthetic Pathways</subject><subject>Humanities and Social Sciences</subject><subject>multidisciplinary</subject><subject>Oxidoreductases Acting on CH-CH Group Donors - chemistry</subject><subject>Oxidoreductases Acting on CH-CH Group Donors - genetics</subject><subject>Oxidoreductases Acting on CH-CH Group Donors - metabolism</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Rhodobacter capsulatus - enzymology</subject><subject>Rhodobacter capsulatus - metabolism</subject><subject>Science</subject><subject>Spectroscopy, Near-Infrared</subject><subject>Substrate Specificity</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><recordid>eNptkV1LHTEQhkOxVLFe9A-UXGph23zsZrM3gkirBaE3eh2S7OzZSE6yTXbV_femHHtQMDcTmIdnhnkR-kLJd0q4_JETTIQy2n5AR4zUTcU4Ywev_ofoJOd7Ul7Dupp2n9Ah41yKruVHaLoIeAnwNIGdofcrNkkHO0KPjYt5DfMIs7N40vP4qFc8xISNLmhy0Y4-pjiNq_fYYKsnbTzgOGBtckzGhQ0OoFPlwpB0KkbvNuP8GX0ctM9w8lKP0d2vn7eX19XNn6vflxc3lW0YmStr-pYTYq2gkggtG9kRyQiwlsteGMplLZiQNZe6t13fCiH40AOlrbDCDIYfo_Odd1rMFnoLYU7aqym5rU6ritqpt53gRrWJD4o3oi53LYLTF0GKfxfIs9q6bMF7HSAuWVEmm7JSI3hBz3aoTTGXPIb9GErUv5DUPqTCfn291578H0kBvu2AXFphA0ndxyWFcqt3bM9A2p4W</recordid><startdate>20130205</startdate><enddate>20130205</enddate><creator>Tsukatani, Yusuke</creator><creator>Yamamoto, Haruki</creator><creator>Harada, Jiro</creator><creator>Yoshitomi, Taichi</creator><creator>Nomata, Jiro</creator><creator>Kasahara, Masahiro</creator><creator>Mizoguchi, Tadashi</creator><creator>Fujita, Yuichi</creator><creator>Tamiaki, Hitoshi</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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><scope>5PM</scope></search><sort><creationdate>20130205</creationdate><title>An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light</title><author>Tsukatani, Yusuke ; Yamamoto, Haruki ; Harada, Jiro ; Yoshitomi, Taichi ; Nomata, Jiro ; Kasahara, Masahiro ; Mizoguchi, Tadashi ; Fujita, Yuichi ; Tamiaki, Hitoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c520t-cbd7300cc61806a85890820e2738d6b13846268438adc9d76663fde1176c6bfb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>631/181/735</topic><topic>631/449/1734</topic><topic>631/45/612/1141</topic><topic>631/61/350</topic><topic>Alphaproteobacteria - enzymology</topic><topic>Alphaproteobacteria - metabolism</topic><topic>Bacteriochlorophyll A - chemistry</topic><topic>Bacteriochlorophyll A - metabolism</topic><topic>Bacteriochlorophylls - chemistry</topic><topic>Bacteriochlorophylls - metabolism</topic><topic>Biosynthetic Pathways</topic><topic>Humanities and Social Sciences</topic><topic>multidisciplinary</topic><topic>Oxidoreductases Acting on CH-CH Group Donors - chemistry</topic><topic>Oxidoreductases Acting on CH-CH Group Donors - genetics</topic><topic>Oxidoreductases Acting on CH-CH Group Donors - metabolism</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Rhodobacter capsulatus - enzymology</topic><topic>Rhodobacter capsulatus - metabolism</topic><topic>Science</topic><topic>Spectroscopy, Near-Infrared</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsukatani, Yusuke</creatorcontrib><creatorcontrib>Yamamoto, Haruki</creatorcontrib><creatorcontrib>Harada, Jiro</creatorcontrib><creatorcontrib>Yoshitomi, Taichi</creatorcontrib><creatorcontrib>Nomata, Jiro</creatorcontrib><creatorcontrib>Kasahara, Masahiro</creatorcontrib><creatorcontrib>Mizoguchi, Tadashi</creatorcontrib><creatorcontrib>Fujita, Yuichi</creatorcontrib><creatorcontrib>Tamiaki, Hitoshi</creatorcontrib><collection>Springer Nature OA Free Journals</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tsukatani, Yusuke</au><au>Yamamoto, Haruki</au><au>Harada, Jiro</au><au>Yoshitomi, Taichi</au><au>Nomata, Jiro</au><au>Kasahara, Masahiro</au><au>Mizoguchi, Tadashi</au><au>Fujita, Yuichi</au><au>Tamiaki, Hitoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2013-02-05</date><risdate>2013</risdate><volume>3</volume><issue>1</issue><spage>1217</spage><epage>1217</epage><pages>1217-1217</pages><artnum>1217</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Chlorophyllous pigments are essential for photosynthesis. Bacteriochlorophyll (BChl)
b
has the characteristic C8-ethylidene group and therefore is the sole naturally occurring pigment having an absorption maximum at near-infrared light wavelength. Here we report that chlorophyllide
a
oxidoreductase (COR), a nitrogenase-like enzyme, showed distinct substrate recognition and catalytic reaction between BChl
a-
and
b
-producing proteobacteria. COR from BChl
b
-producing
Blastochloris viridis
synthesized the C8-ethylidene group from 8-vinyl-chlorophyllide
a
. In contrast, despite the highly conserved primary structures, COR from BChl
a
-producing
Rhodobacter capsulatus
catalyzes the C8-vinyl reduction as well as the previously known reaction of the C7 = C8 double bond reduction on 8-vinyl-chlorophyllide
a
. The present data indicate that the plasticity of the nitrogenase-like enzyme caused the branched pathways of BChls
a
and
b
biosynthesis, ultimately leading to ecologically different niches of BChl
a
- and
b
-based photosynthesis differentiated by more than 150 nm wavelength.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>23386973</pmid><doi>10.1038/srep01217</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2013-02, Vol.3 (1), p.1217-1217, Article 1217 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3564038 |
| source | MEDLINE; Nature Free; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry; Springer Nature OA Free Journals |
| subjects | 631/181/735 631/449/1734 631/45/612/1141 631/61/350 Alphaproteobacteria - enzymology Alphaproteobacteria - metabolism Bacteriochlorophyll A - chemistry Bacteriochlorophyll A - metabolism Bacteriochlorophylls - chemistry Bacteriochlorophylls - metabolism Biosynthetic Pathways Humanities and Social Sciences multidisciplinary Oxidoreductases Acting on CH-CH Group Donors - chemistry Oxidoreductases Acting on CH-CH Group Donors - genetics Oxidoreductases Acting on CH-CH Group Donors - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - genetics Rhodobacter capsulatus - enzymology Rhodobacter capsulatus - metabolism Science Spectroscopy, Near-Infrared Substrate Specificity |
| title | An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light |
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