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  1. Book ; Online ; Thesis: Shedding light on protein-chromophore-interactions: spectroscopy-based characterization of carotenoid binding in the orange carotenoid protein

    Moldenhauer, Marcus [Verfasser] / Friedrich, Thomas [Akademischer Betreuer] / Friedrich, Thomas [Gutachter] / Lohr, Martin [Gutachter]

    2024  

    Author's details Marcus Moldenhauer ; Gutachter: Thomas Friedrich, Martin Lohr ; Betreuer: Thomas Friedrich
    Keywords Naturwissenschaften ; Science
    Subject code sg500
    Language English
    Publisher Technische Universität Berlin
    Publishing place Berlin
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  2. Article ; Online: Extraction and Analysis of Carotenoids from

    Blatt, Andreas / Lohr, Martin

    Bio-protocol

    2017  Volume 7, Issue 6, Page(s) e2179

    Abstract: A common method to investigate the function of genes putatively involved in carotenoid biosynthesis is the so called color complementation assay ... ...

    Abstract A common method to investigate the function of genes putatively involved in carotenoid biosynthesis is the so called color complementation assay in
    Language English
    Publishing date 2017-03-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2833269-6
    ISSN 2331-8325 ; 2331-8325
    ISSN (online) 2331-8325
    ISSN 2331-8325
    DOI 10.21769/BioProtoc.2179
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: A functional zeaxanthin epoxidase from red algae shedding light on the evolution of light-harvesting carotenoids and the xanthophyll cycle in photosynthetic eukaryotes.

    Dautermann, Oliver / Lohr, Martin

    The Plant journal : for cell and molecular biology

    2017  Volume 92, Issue 5, Page(s) 879–891

    Abstract: The epoxy-xanthophylls antheraxanthin and violaxanthin are key precursors of light-harvesting carotenoids and participate in the photoprotective xanthophyll cycle. Thus, the invention of zeaxanthin epoxidase (ZEP) catalyzing their formation from ... ...

    Abstract The epoxy-xanthophylls antheraxanthin and violaxanthin are key precursors of light-harvesting carotenoids and participate in the photoprotective xanthophyll cycle. Thus, the invention of zeaxanthin epoxidase (ZEP) catalyzing their formation from zeaxanthin has been a fundamental step in the evolution of photosynthetic eukaryotes. ZEP genes have only been found in Viridiplantae and chromalveolate algae with secondary plastids of red algal ancestry, suggesting that ZEP evolved in the Viridiplantae and spread to chromalveolates by lateral gene transfer. By searching publicly available sequence data from 11 red algae covering all currently recognized red algal classes we identified ZEP candidates in three species. Phylogenetic analyses showed that the red algal ZEP is most closely related to ZEP proteins from photosynthetic chromalveolates possessing secondary plastids of red algal origin. Its enzymatic activity was assessed by high performance liquid chromatography (HPLC) analyses of red algal pigment extracts and by cloning and functional expression of the ZEP gene from Madagascaria erythrocladioides in leaves of the ZEP-deficient aba2 mutant of Nicotiana plumbaginifolia. Unlike other ZEP enzymes examined so far, the red algal ZEP introduces only a single epoxy group into zeaxanthin, yielding antheraxanthin instead of violaxanthin. The results indicate that ZEP evolved before the split of Rhodophyta and Viridiplantae and that chromalveolates acquired ZEP from the red algal endosymbiont and not by lateral gene transfer. Moreover, the red algal ZEP enables engineering of transgenic plants incorporating antheraxanthin instead of violaxanthin in their photosynthetic machinery.
    Language English
    Publishing date 2017-12
    Publishing country England
    Document type Journal Article
    ZDB-ID 1088037-9
    ISSN 1365-313X ; 0960-7412
    ISSN (online) 1365-313X
    ISSN 0960-7412
    DOI 10.1111/tpj.13725
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: A multi-center international study to evaluate the safety, functional and oncological outcomes of irreversible electroporation for the ablation of prostate cancer.

    Zhang, Kai / Stricker, Phillip / Löhr, Martin / Stehling, Michael / Suberville, Michel / Cussenot, Olivier / Lunelli, Luca / Ng, Chi-Fai / Teoh, Jeremy / Laguna, Pilar / de la Rosette, Jean

    Prostate cancer and prostatic diseases

    2024  

    Abstract: Background: Irreversible electroporation (IRE) is a novel technique to treat localized prostate cancer with the aim of achieving oncological control while reducing related side effects. We present the outcomes of localized prostate cancer treated with ... ...

    Abstract Background: Irreversible electroporation (IRE) is a novel technique to treat localized prostate cancer with the aim of achieving oncological control while reducing related side effects. We present the outcomes of localized prostate cancer treated with IRE from a multi-center prospective registry.
    Methods: Men with histologically confirmed prostate cancer were recruited to receive IRE. All the patients were proposed for prostate biopsy at 1-year post-IRE ablation. The functional outcomes were measured by the International Prostate Symptom Score (IPSS) and International Index of Erectile Function (IIEF-5) questionnaires. The safety of IRE was graded by the treatment-related adverse events (AEs) according to the Common Terminology Criteria for Adverse Events (CTCAE).
    Results: 411 patients were recruited in this study from July 2015 to April 2020. The median follow-up time was 24 months (IQR 15-36). 116 patients underwent repeat prostate biopsy during 12-18 months after IRE. Clinically significant prostate cancer (Gleason ≥ 3 + 4) was detected in 24.1% (28/116) of the patients; any grade prostate cancers were found in 59.5% (69/116) of the patients. The IPSS score increased significantly from 7.1 to 8.2 (p = 0.015) at 3 months but decreased to 6.1 at 6 months (p = 0.017). Afterwards, the IPSS level remained stable during follow-up. The IIEF-5 score decreased at 3 months from 16.0 to 12.1 (p < 0.001) and then maintained equable afterwards. The rate of AEs was 1.8% at 3 months and then dropped to less than 1% at 6 months and remained stable until 48 months after IRE. Major AEs (Grade 3 or above) were rare.
    Conclusion: For men with localized prostate cancer, IRE could achieve good urinary and sexual function outcomes and a reasonable oncological result. The real-world data are consistent with earlier studies, including recently published randomized controlled studies. The long-term oncological results need further investigation and follow-up.
    Language English
    Publishing date 2024-01-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 1419277-9
    ISSN 1476-5608 ; 1365-7852
    ISSN (online) 1476-5608
    ISSN 1365-7852
    DOI 10.1038/s41391-023-00783-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Green diatom mutants reveal an intricate biosynthetic pathway of fucoxanthin.

    Bai, Yu / Cao, Tianjun / Dautermann, Oliver / Buschbeck, Paul / Cantrell, Michael B / Chen, Yinjuan / Lein, Christopher D / Shi, Xiaohuo / Ware, Maxwell A / Yang, Fenghua / Zhang, Huan / Zhang, Lihan / Peers, Graham / Li, Xiaobo / Lohr, Martin

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 38, Page(s) e2203708119

    Abstract: Fucoxanthin is a major light-harvesting pigment in ecologically important algae such as diatoms, haptophytes, and brown algae (Phaeophyceae). Therefore, it is a major driver of global primary productivity. Species of these algal groups are brown colored ... ...

    Abstract Fucoxanthin is a major light-harvesting pigment in ecologically important algae such as diatoms, haptophytes, and brown algae (Phaeophyceae). Therefore, it is a major driver of global primary productivity. Species of these algal groups are brown colored because the high amounts of fucoxanthin bound to the proteins of their photosynthetic machineries enable efficient absorption of green light. While the structure of these fucoxanthin-chlorophyll proteins has recently been resolved, the biosynthetic pathway of fucoxanthin is still unknown. Here, we identified two enzymes central to this pathway by generating corresponding knockout mutants of the diatom
    MeSH term(s) Biosynthetic Pathways/genetics ; Carotenoids/metabolism ; Diatoms/genetics ; Diatoms/metabolism ; Phaeophyceae/metabolism ; Xanthophylls/metabolism
    Chemical Substances Xanthophylls ; fucoxanthin (06O0TC0VSM) ; Carotenoids (36-88-4)
    Language English
    Publishing date 2022-09-12
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2203708119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Book ; Online ; Thesis: Beziehungen zwischen den Xanthophyllzyklen und der Biosynthese von Lichtsammelxanthophyllen in Chlorophyll-a-c-haltigen Algen

    Lohr, Martin

    2000  

    Author's details Martin Lohr
    Keywords Biosynthese ; Chromophyta ; Xanthophyllzyklus ; Xanthophylle
    Language German
    Size Online-Ressource
    Edition [Elektronische Ressource]
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss--Mainz, 2001
    Database Former special subject collection: coastal and deep sea fishing

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  7. Article ; Online: An unexpected hydratase synthesizes the green light-absorbing pigment fucoxanthin.

    Cao, Tianjun / Bai, Yu / Buschbeck, Paul / Tan, Qiaozhu / Cantrell, Michael B / Chen, Yinjuan / Jiang, Yanyou / Liu, Run-Zhou / Ries, Nana K / Shi, Xiaohuo / Sun, Yan / Ware, Maxwell A / Yang, Fenghua / Zhang, Huan / Han, Jichang / Zhang, Lihan / Huang, Jing / Lohr, Martin / Peers, Graham /
    Li, Xiaobo

    The Plant cell

    2023  Volume 35, Issue 8, Page(s) 3053–3072

    Abstract: The ketocarotenoid fucoxanthin and its derivatives can absorb blue-green light enriched in marine environments. Fucoxanthin is widely adopted by phytoplankton species as a main light-harvesting pigment, in contrast to land plants that primarily employ ... ...

    Abstract The ketocarotenoid fucoxanthin and its derivatives can absorb blue-green light enriched in marine environments. Fucoxanthin is widely adopted by phytoplankton species as a main light-harvesting pigment, in contrast to land plants that primarily employ chlorophylls. Despite its supreme abundance in the oceans, the last steps of fucoxanthin biosynthesis have remained elusive. Here, we identified the carotenoid isomerase-like protein CRTISO5 as the diatom fucoxanthin synthase that is related to the carotenoid cis-trans isomerase CRTISO from land plants but harbors unexpected enzymatic activity. A crtiso5 knockout mutant in the model diatom Phaeodactylum tricornutum completely lacked fucoxanthin and accumulated the acetylenic carotenoid phaneroxanthin. Recombinant CRTISO5 converted phaneroxanthin into fucoxanthin in vitro by hydrating its carbon-carbon triple bond, instead of functioning as an isomerase. Molecular docking and mutational analyses revealed residues essential for this activity. Furthermore, a photophysiological characterization of the crtiso5 mutant revealed a major structural and functional role of fucoxanthin in photosynthetic pigment-protein complexes of diatoms. As CRTISO5 hydrates an internal alkyne physiologically, the enzyme has unique potential for biocatalytic applications. The discovery of CRTISO5 illustrates how neofunctionalization leads to major diversification events in evolution of photosynthetic mechanisms and the prominent brown coloration of most marine photosynthetic eukaryotes.
    MeSH term(s) Molecular Docking Simulation ; Xanthophylls/metabolism ; Carotenoids/metabolism ; Chlorophyll/metabolism ; Diatoms/genetics ; Diatoms/metabolism
    Chemical Substances fucoxanthin (06O0TC0VSM) ; Xanthophylls ; Carotenoids (36-88-4) ; Chlorophyll (1406-65-1)
    Language English
    Publishing date 2023-04-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 623171-8
    ISSN 1532-298X ; 1040-4651
    ISSN (online) 1532-298X
    ISSN 1040-4651
    DOI 10.1093/plcell/koad116
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: A lycopene β-cyclase/lycopene ε-cyclase/light-harvesting complex-fusion protein from the green alga Ostreococcus lucimarinus can be modified to produce α-carotene and β-carotene at different ratios.

    Blatt, Andreas / Bauch, Matthias E / Pörschke, Yvonne / Lohr, Martin

    The Plant journal : for cell and molecular biology

    2015  Volume 82, Issue 4, Page(s) 582–595

    Abstract: Biosynthesis of asymmetric carotenoids such as α-carotene and lutein in plants and green algae involves the two enzymes lycopene β-cyclase (LCYB) and lycopene ε-cyclase (LCYE). The two cyclases are closely related and probably resulted from an ancient ... ...

    Abstract Biosynthesis of asymmetric carotenoids such as α-carotene and lutein in plants and green algae involves the two enzymes lycopene β-cyclase (LCYB) and lycopene ε-cyclase (LCYE). The two cyclases are closely related and probably resulted from an ancient gene duplication. While in most plants investigated so far the two cyclases are encoded by separate genes, prasinophyte algae of the order Mamiellales contain a single gene encoding a fusion protein comprised of LCYB, LCYE and a C-terminal light-harvesting complex (LHC) domain. Here we show that the lycopene cyclase fusion protein from Ostreococcus lucimarinus catalyzed the simultaneous formation of α-carotene and β-carotene when heterologously expressed in Escherichia coli. The stoichiometry of the two products in E. coli could be altered by gradual truncation of the C-terminus, suggesting that the LHC domain may be involved in modulating the relative activities of the two cyclase domains in the algae. Partial deletions of the linker region between the cyclase domains or replacement of one or both cyclase domains with the corresponding cyclases from the green alga Chlamydomonas reinhardtii resulted in pronounced shifts of the α-carotene-to-β-carotene ratio, indicating that both the relative activities of the cyclase domains and the overall structure of the fusion protein have a strong impact on the product stoichiometry. The possibility to tune the product ratio of the lycopene cyclase fusion protein from Mamiellales renders it useful for the biotechnological production of the asymmetric carotenoids α-carotene or lutein in bacteria or fungi.
    MeSH term(s) Carotenoids/metabolism ; Chlorophyta/enzymology ; Chlorophyta/genetics ; Chlorophyta/metabolism ; Intramolecular Lyases/genetics ; Intramolecular Lyases/metabolism ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; beta Carotene/metabolism
    Chemical Substances Plant Proteins ; Recombinant Fusion Proteins ; beta Carotene (01YAE03M7J) ; Carotenoids (36-88-4) ; alpha-carotene (45XWE1Z69V) ; Intramolecular Lyases (EC 5.5.-) ; lycopene cyclase-isomerase (EC 5.5.-)
    Language English
    Publishing date 2015-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1088037-9
    ISSN 1365-313X ; 0960-7412
    ISSN (online) 1365-313X
    ISSN 0960-7412
    DOI 10.1111/tpj.12826
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Isoprenoid biosynthesis in eukaryotic phototrophs: A spotlight on algae

    Lohr, Martin / Schwender, Jörg / Polle, Jürgen E.W

    Plant science. 2012 Apr., v. 185-186

    2012  

    Abstract: Isoprenoids are one of the largest groups of natural compounds and have a variety of important functions in the primary metabolism of land plants and algae. In recent years, our understanding of the numerous facets of isoprenoid metabolism in land plants ...

    Abstract Isoprenoids are one of the largest groups of natural compounds and have a variety of important functions in the primary metabolism of land plants and algae. In recent years, our understanding of the numerous facets of isoprenoid metabolism in land plants has been rapidly increasing, while knowledge on the metabolic network of isoprenoids in algae still lags behind. Here, current views on the biochemistry and genetics of the core isoprenoid metabolism in land plants and in the major algal phyla are compared and some of the most pressing open questions are highlighted. Based on the different evolutionary histories of the various groups of eukaryotic phototrophs, we discuss the distribution and regulation of the mevalonate (MVA) and the methylerythritol phosphate (MEP) pathways in land plants and algae and the potential consequences of the loss of the MVA pathway in groups such as the green algae. For the prenyltransferases, serving as gatekeepers to the various branches of terpenoid biosynthesis in land plants and algae, we explore the minimal inventory necessary for the formation of primary isoprenoids and present a preliminary analysis of their occurrence and phylogeny in algae with primary and secondary plastids. The review concludes with some perspectives on genetic engineering of the isoprenoid metabolism in algae.
    Keywords Chlorophycota ; autotrophs ; biosynthesis ; embryophytes ; genetic engineering ; inventories ; isoprenoids ; phylogeny ; plastids
    Language English
    Dates of publication 2012-04
    Size p. 9-22.
    Publishing place Elsevier Ireland Ltd
    Document type Article
    ZDB-ID 742010-9
    ISSN 1873-2259 ; 0168-9452
    ISSN (online) 1873-2259
    ISSN 0168-9452
    DOI 10.1016/j.plantsci.2011.07.018
    Database NAL-Catalogue (AGRICOLA)

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  10. Book: Biosynthese von Xanthophyllen in Gruenalgen und Kieselalgen

    Lohr, Martin

    Abstract: Nachdem in Gefaesspflanzen die an der Carotinoidbiosynthese in den photosynthetisch aktiven Organen beteiligten Enzyme inzwischen weitestgehend identifiziert worden sind, soll im hier beantragten Projekt die Carotinoidbiosynthese in der Gruenalge ... ...

    Institution Universitaet Mainz, Institut fuer Allgemeine Botanik, Muellerweg 6, 55099, Mainz, DE
    Abstract Nachdem in Gefaesspflanzen die an der Carotinoidbiosynthese in den photosynthetisch aktiven Organen beteiligten Enzyme inzwischen weitestgehend identifiziert worden sind, soll im hier beantragten Projekt die Carotinoidbiosynthese in der Gruenalge Chlamydomonas reinhardtii und der Diatomee Phaeodactylum tricornutum untersucht werden. Hierzu sind zunaechst die Identifizierung von an der Xanthophyllbiosynthese beteiligten Gene aus beiden Algen sowie die Isolierung und Charakterisierung neuer Pigmentmutanten von C.reinhardtii vorgesehen. Besonderes Augenmerk liegt ferner auf der Identifizierung einer Diadinoxanthin-Synthase (DDS) aus P.tricornutum. Die bereits vorliegenden sowie die neu isolierten Pigmentmutanten von C. reinhardtii sollen als Testsystem fuer die Funktion potentieller Xanthophyllbiosynthesegene aus beiden Algen eingesetzt werden. Die DDS aus P.tricornutum soll anschliessend in einem bakteriellen System sowie in C.reinhardtii exprimiert, isoliert und bezueglich ihrer katalytischen Eigenschaften eingehend charakterisiert werden. Eine erfolgreiche funktionelle Expression der DDS in C. reinhardtii wuerde in der Synthese eines bislang in Gruenalgen nicht vorkommenden Xanthophylls resultieren. Hiervon waeren neue Erkenntnisse hinsichtlich der Flexibilitaet der Pigmentbindungseigenschaften von Lichtsammelkomplexen sowie der Funktion und Evolution des Diadinoxanthinzyklus zu erwarten.
    Keywords Biosynthese ; Gruenalgen ; Gefaesspflanze ; Enzym ; Diatomeen ; Gen ; Algen ; Isolierung ; Synthese ; Evolution ; Wasserorganismen ; Pigment ; Chlorophyll ; Photosynthese ; Pflanzenwachstum
    Language German
    Document type Book
    Remark Projektbeginn: 14.06.2001 Projektende: Foerdernummer:
    Database Environmental research database (UFORDAT) of the German Federal Environment Agency (UBA)

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