Studies on the Functional Mechanism of System II Herbicides in Isolated Chloroplasts
| dc.contributor.author | Renger, Gernot | |
| dc.contributor.author | Hagemann, A. | |
| dc.contributor.author | Vermaas, Wim F.J. | |
| dc.date.accessioned | 2019-01-02T14:02:03Z | |
| dc.date.available | 2019-01-02T14:02:03Z | |
| dc.date.issued | 1984 | |
| dc.description.abstract | The effect of specific proteolytic enzymes on variable fluorescence, p-benzoquinone-mediated oxygen evolution, PS II herbicide (atrazine and bromoxynil) binding, and protein degradation has been analyzed in isolated class II pea chloroplasts. It was found that: 1. Trypsin and a lysine-specific protease effectively reduce the maximum chlorophyll-a fluorescence yield, whereas the initial fluorescence remains almost constant. At the same number of enzymatic activity units both proteases have practically the same effect. 2. Trypsin and a lysine-specific protease inhibit the p-benzoquinone-mediated flash-induced oxygen evolution with trypsin being markedly more effective at the same number of activity units of both enzymes. Unstacked thylakoids exhibit a higher sensitivity to proteolytic degradation by both enzymes. 3. Trypsin and a lysine-specific protease reduce the binding capacity of [14C]atrazine, but enhance that of [14C]bromoxynil (at long incubation times trypsin treatment also impairs bromoxynil binding). At the same specific activity a markedly longer treatment is required for the lysine-specific protease in order to achieve the same degree of modification as with trypsin. 4. Trypsin was found to attack the rapidly-turned-over 32 kDa-protein severely, whereas the lysine-specific protease does not modify this polypeptide. On the other hand, the lysine-specific protease attacks the light harvesting complex II. 5. Under our experimental conditions an arginine-specific protease did not affect chlorophyll-a fluorescence yield, p-benzoquinone-mediated oxygen evolution, herbicide binding and the poly- peptide pattern. Based on these results a mechanism is proposed in which an as yet unidentified polypeptide with exposable lysine residues, as well as the lysine-free “QB-protein” regulate the electron transfer from Q-A to QB and are involved in herbicide binding. | en |
| dc.identifier.eissn | 1865-7125 | |
| dc.identifier.issn | 0939-5075 | |
| dc.identifier.uri | https://depositonce.tu-berlin.de/handle/11303/8775 | |
| dc.identifier.uri | http://dx.doi.org/10.14279/depositonce-7904 | |
| dc.language.iso | en | |
| dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/ | |
| dc.subject.ddc | 570 Biowissenschaften; Biologie | de |
| dc.subject.other | chloroplasts | en |
| dc.subject.other | proteolytic enzymes | en |
| dc.subject.other | fluorescence | en |
| dc.subject.other | oxygen evolution | en |
| dc.subject.other | herbicide binding | en |
| dc.title | Studies on the Functional Mechanism of System II Herbicides in Isolated Chloroplasts | en |
| dc.type | Article | en |
| dc.type.version | publishedVersion | en |
| dcterms.bibliographicCitation.doi | 10.1515/znc-1984-0510 | |
| dcterms.bibliographicCitation.issue | 5 | |
| dcterms.bibliographicCitation.journaltitle | Zeitschrift für Naturforschung C | de |
| dcterms.bibliographicCitation.originalpublishername | De Gruyter | en |
| dcterms.bibliographicCitation.originalpublisherplace | Berlin | |
| dcterms.bibliographicCitation.pageend | 367 | |
| dcterms.bibliographicCitation.pagestart | 362 | |
| dcterms.bibliographicCitation.volume | 39 | |
| tub.accessrights.dnb | free | |
| tub.affiliation | Fak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemie | de |
| tub.affiliation.faculty | Fak. 2 Mathematik und Naturwissenschaften | de |
| tub.affiliation.group | FG Physikalische Chemie / Biophysikalische Chemie | de |
| tub.affiliation.institute | Inst. Chemie | de |
| tub.publisher.universityorinstitution | Technische Universität Berlin | de |
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