Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle
This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. PO...
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| Autor*in: |
PEARSE, IAN S. [verfasserIn] HEATH, KATY D. [verfasserIn] CHEESEMAN, JOHN M. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Science Ltd ; 2005 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2005 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: Plant, cell & environment - Oxford [u.a.] : Wiley-Blackwell, 1978, 28(2005), 5, Seite 0 |
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volume:28 ; year:2005 ; number:5 ; pages:0 |
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| DOI / URN: |
10.1111/j.1365-3040.2005.01307.x |
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| 520 | |a This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. | ||
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10.1111/j.1365-3040.2005.01307.x doi (DE-627)NLEJ243837232 DE-627 ger DE-627 rakwb PEARSE, IAN S. verfasserin aut Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle Oxford, UK Blackwell Science Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. 2005 Blackwell Publishing Journal Backfiles 1879-2005 |2005|||||||||| Belize HEATH, KATY D. verfasserin aut CHEESEMAN, JOHN M. verfasserin aut In Plant, cell & environment Oxford [u.a.] : Wiley-Blackwell, 1978 28(2005), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926944 (DE-600)2020843-1 1365-3040 nnns volume:28 year:2005 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-3040.2005.01307.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 28 2005 5 0 |
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10.1111/j.1365-3040.2005.01307.x doi (DE-627)NLEJ243837232 DE-627 ger DE-627 rakwb PEARSE, IAN S. verfasserin aut Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle Oxford, UK Blackwell Science Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. 2005 Blackwell Publishing Journal Backfiles 1879-2005 |2005|||||||||| Belize HEATH, KATY D. verfasserin aut CHEESEMAN, JOHN M. verfasserin aut In Plant, cell & environment Oxford [u.a.] : Wiley-Blackwell, 1978 28(2005), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926944 (DE-600)2020843-1 1365-3040 nnns volume:28 year:2005 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-3040.2005.01307.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 28 2005 5 0 |
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10.1111/j.1365-3040.2005.01307.x doi (DE-627)NLEJ243837232 DE-627 ger DE-627 rakwb PEARSE, IAN S. verfasserin aut Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle Oxford, UK Blackwell Science Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. 2005 Blackwell Publishing Journal Backfiles 1879-2005 |2005|||||||||| Belize HEATH, KATY D. verfasserin aut CHEESEMAN, JOHN M. verfasserin aut In Plant, cell & environment Oxford [u.a.] : Wiley-Blackwell, 1978 28(2005), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926944 (DE-600)2020843-1 1365-3040 nnns volume:28 year:2005 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-3040.2005.01307.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 28 2005 5 0 |
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10.1111/j.1365-3040.2005.01307.x doi (DE-627)NLEJ243837232 DE-627 ger DE-627 rakwb PEARSE, IAN S. verfasserin aut Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle Oxford, UK Blackwell Science Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. 2005 Blackwell Publishing Journal Backfiles 1879-2005 |2005|||||||||| Belize HEATH, KATY D. verfasserin aut CHEESEMAN, JOHN M. verfasserin aut In Plant, cell & environment Oxford [u.a.] : Wiley-Blackwell, 1978 28(2005), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926944 (DE-600)2020843-1 1365-3040 nnns volume:28 year:2005 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-3040.2005.01307.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 28 2005 5 0 |
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10.1111/j.1365-3040.2005.01307.x doi (DE-627)NLEJ243837232 DE-627 ger DE-627 rakwb PEARSE, IAN S. verfasserin aut Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle Oxford, UK Blackwell Science Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. 2005 Blackwell Publishing Journal Backfiles 1879-2005 |2005|||||||||| Belize HEATH, KATY D. verfasserin aut CHEESEMAN, JOHN M. verfasserin aut In Plant, cell & environment Oxford [u.a.] : Wiley-Blackwell, 1978 28(2005), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926944 (DE-600)2020843-1 1365-3040 nnns volume:28 year:2005 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-3040.2005.01307.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 28 2005 5 0 |
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biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, rhizophora mangle |
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Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle |
| abstract |
This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. |
| abstractGer |
This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. |
| abstract_unstemmed |
This study examines phenolic peroxidase (POX) in Rhizophora mangle L. leaves in order to assess its role in phenolic manipulation and H2O2 scavenging. Sun-exposed and understorey leaves experiencing varying degrees of nutrient stress were analysed from an oligotrophic cay off the coast of Belize. POX activity was unaffected by growth environment, but increased throughout leaf development and persisted through senescence and after abscission. Histochemical analyses indicated POX activity throughout leaf tissues, especially in the apoplast. Phenolics were similarly broadly distributed. Two isoenzymes of POX were partially characterized with pIs of 4.1 and 6.3 and masses of 65.5 and 54.3 kDa, respectively. The larger, more acidic isoenzyme showed especially high heat stability, showing no reduced activity after 24 h at 60 °C. Rhizophora mangle POX oxidized quercetin preferentially, and, to a lesser extent, coniferyl alcohol, caffeic acid, chlorogenic acid, and p-coumaric acid. It did not oxidize ascorbate, but ascorbate could act as a secondary electron donor in the presence of a phenolic substrate and H2O2. However, because quercetin and other aglycones were not present in R. mangle leaves, and because POX showed no activity with the most abundant leaf flavonoid, rutin, it was concluded that detoxification of H2O2 is secondary to the other roles of POX in manipulation of phenolics. |
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Biochemical and ecological characterization of two peroxidase isoenzymes from the mangrove, Rhizophora mangle |
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HEATH, KATY D. CHEESEMAN, JOHN M. |
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