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Polyphenol Oxidation by Vicia faba Chloroplast Membranes: STUDIES ON THE LATENT MEMBRANE-BOUND POLYPHENOL OXIDASE AND ON THE MECHANISM
The mechanism whereby light effects polyphenol oxidation was examined with Vicia faba chloroplast membranes known to contain a bound latent polyphenol oxidase. Results obtained with the inhibitors 3-(3′,4′-dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-idopropyl- p -benzoquinone...
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Published in: | Plant physiology (Bethesda) 1980-12, Vol.66 (6), p.1150-1154 |
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container_title | Plant physiology (Bethesda) |
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creator | Hutcheson, Steven W. Buchanan, Bob B. Montalbini, Paolo |
description | The mechanism whereby light effects polyphenol oxidation was examined with
Vicia faba
chloroplast membranes known to contain a bound latent polyphenol oxidase. Results obtained with the inhibitors 3-(3′,4′-dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-idopropyl-
p
-benzoquinone (DBMIB) indicated an involvement of the non-cyclic electron transport pathway in the light-dependent oxidation of polyphenols, such as dihydroxyphenylalanine (DOPA). Further evidence was provided by experiments in which (
a
) DOPA replaced H
2
O as electron donor for the photoreduction of NADP, (
b
) NADP replaced O
2
as electron acceptor in the photochemical oxidation of DOPA, and (
c
) the variable fluorescence associated with photosystem II was increased by DOPA. The photochemical oxidation of DOPA by
V. faba
chloroplast membranes was insensitive to KCN and to antibodies against purified latent polyphenol oxidase. The results are consistent with the conclusion that the light-dependent oxidation of polyphenols by
V. faba
chloroplast membranes is achieved independently of the latent membrane-bound polyphenol oxidase. Electrons derived from polyphenols seem to enter the noncyclic electron transport chain on the oxidizing side of photosystem II and to react with O
2
at an unidentified site on the photosystem I side of the DCMU/DBMIB blocks.
The physiological mechanism for the activation of latent polyphenol oxidase remains an unanswered question. Present results suggest that activation could occur through either acidification or the release of free fatty acids. |
format | article |
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Vicia faba
chloroplast membranes known to contain a bound latent polyphenol oxidase. Results obtained with the inhibitors 3-(3′,4′-dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-idopropyl-
p
-benzoquinone (DBMIB) indicated an involvement of the non-cyclic electron transport pathway in the light-dependent oxidation of polyphenols, such as dihydroxyphenylalanine (DOPA). Further evidence was provided by experiments in which (
a
) DOPA replaced H
2
O as electron donor for the photoreduction of NADP, (
b
) NADP replaced O
2
as electron acceptor in the photochemical oxidation of DOPA, and (
c
) the variable fluorescence associated with photosystem II was increased by DOPA. The photochemical oxidation of DOPA by
V. faba
chloroplast membranes was insensitive to KCN and to antibodies against purified latent polyphenol oxidase. The results are consistent with the conclusion that the light-dependent oxidation of polyphenols by
V. faba
chloroplast membranes is achieved independently of the latent membrane-bound polyphenol oxidase. Electrons derived from polyphenols seem to enter the noncyclic electron transport chain on the oxidizing side of photosystem II and to react with O
2
at an unidentified site on the photosystem I side of the DCMU/DBMIB blocks.
The physiological mechanism for the activation of latent polyphenol oxidase remains an unanswered question. Present results suggest that activation could occur through either acidification or the release of free fatty acids.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>PMID: 16661594</identifier><language>eng</language><ispartof>Plant physiology (Bethesda), 1980-12, Vol.66 (6), p.1150-1154</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,777,781,882</link.rule.ids></links><search><creatorcontrib>Hutcheson, Steven W.</creatorcontrib><creatorcontrib>Buchanan, Bob B.</creatorcontrib><creatorcontrib>Montalbini, Paolo</creatorcontrib><title>Polyphenol Oxidation by Vicia faba Chloroplast Membranes: STUDIES ON THE LATENT MEMBRANE-BOUND POLYPHENOL OXIDASE AND ON THE MECHANISM</title><title>Plant physiology (Bethesda)</title><description>The mechanism whereby light effects polyphenol oxidation was examined with
Vicia faba
chloroplast membranes known to contain a bound latent polyphenol oxidase. Results obtained with the inhibitors 3-(3′,4′-dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-idopropyl-
p
-benzoquinone (DBMIB) indicated an involvement of the non-cyclic electron transport pathway in the light-dependent oxidation of polyphenols, such as dihydroxyphenylalanine (DOPA). Further evidence was provided by experiments in which (
a
) DOPA replaced H
2
O as electron donor for the photoreduction of NADP, (
b
) NADP replaced O
2
as electron acceptor in the photochemical oxidation of DOPA, and (
c
) the variable fluorescence associated with photosystem II was increased by DOPA. The photochemical oxidation of DOPA by
V. faba
chloroplast membranes was insensitive to KCN and to antibodies against purified latent polyphenol oxidase. The results are consistent with the conclusion that the light-dependent oxidation of polyphenols by
V. faba
chloroplast membranes is achieved independently of the latent membrane-bound polyphenol oxidase. Electrons derived from polyphenols seem to enter the noncyclic electron transport chain on the oxidizing side of photosystem II and to react with O
2
at an unidentified site on the photosystem I side of the DCMU/DBMIB blocks.
The physiological mechanism for the activation of latent polyphenol oxidase remains an unanswered question. Present results suggest that activation could occur through either acidification or the release of free fatty acids.</description><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><recordid>eNqli70OgjAYABujEfx5h74ASQsFy-BENC5GB-PafECRmtKSFo28vQ4uzk53yeUmKKRpEkdxyvgUhYR8nHCeB2jh_Z0QQhPK5iigWZbRNGch4merx76Vxmp8eqkaBmUNLkd8VZUC3EAJuGi1dbbX4Ad8lF3pwEi_QrMGtJfrL5dou99dikPUP8pO1pU0gwMteqc6cKOwoMRvMaoVN_sUjBFONsm__xtb2k_W</recordid><startdate>19801201</startdate><enddate>19801201</enddate><creator>Hutcheson, Steven W.</creator><creator>Buchanan, Bob B.</creator><creator>Montalbini, Paolo</creator><scope>5PM</scope></search><sort><creationdate>19801201</creationdate><title>Polyphenol Oxidation by Vicia faba Chloroplast Membranes</title><author>Hutcheson, Steven W. ; Buchanan, Bob B. ; Montalbini, Paolo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-pubmedcentral_primary_oai_pubmedcentral_nih_gov_4408073</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hutcheson, Steven W.</creatorcontrib><creatorcontrib>Buchanan, Bob B.</creatorcontrib><creatorcontrib>Montalbini, Paolo</creatorcontrib><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hutcheson, Steven W.</au><au>Buchanan, Bob B.</au><au>Montalbini, Paolo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polyphenol Oxidation by Vicia faba Chloroplast Membranes: STUDIES ON THE LATENT MEMBRANE-BOUND POLYPHENOL OXIDASE AND ON THE MECHANISM</atitle><jtitle>Plant physiology (Bethesda)</jtitle><date>1980-12-01</date><risdate>1980</risdate><volume>66</volume><issue>6</issue><spage>1150</spage><epage>1154</epage><pages>1150-1154</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><abstract>The mechanism whereby light effects polyphenol oxidation was examined with
Vicia faba
chloroplast membranes known to contain a bound latent polyphenol oxidase. Results obtained with the inhibitors 3-(3′,4′-dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-idopropyl-
p
-benzoquinone (DBMIB) indicated an involvement of the non-cyclic electron transport pathway in the light-dependent oxidation of polyphenols, such as dihydroxyphenylalanine (DOPA). Further evidence was provided by experiments in which (
a
) DOPA replaced H
2
O as electron donor for the photoreduction of NADP, (
b
) NADP replaced O
2
as electron acceptor in the photochemical oxidation of DOPA, and (
c
) the variable fluorescence associated with photosystem II was increased by DOPA. The photochemical oxidation of DOPA by
V. faba
chloroplast membranes was insensitive to KCN and to antibodies against purified latent polyphenol oxidase. The results are consistent with the conclusion that the light-dependent oxidation of polyphenols by
V. faba
chloroplast membranes is achieved independently of the latent membrane-bound polyphenol oxidase. Electrons derived from polyphenols seem to enter the noncyclic electron transport chain on the oxidizing side of photosystem II and to react with O
2
at an unidentified site on the photosystem I side of the DCMU/DBMIB blocks.
The physiological mechanism for the activation of latent polyphenol oxidase remains an unanswered question. Present results suggest that activation could occur through either acidification or the release of free fatty acids.</abstract><pmid>16661594</pmid></addata></record> |
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language | eng |
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source | JSTOR Archival Journals and Primary Sources Collection; Alma/SFX Local Collection |
title | Polyphenol Oxidation by Vicia faba Chloroplast Membranes: STUDIES ON THE LATENT MEMBRANE-BOUND POLYPHENOL OXIDASE AND ON THE MECHANISM |
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