Relevant bibliographies by topics / Protochlorophyllide

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
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Academic literature on the topic 'Protochlorophyllide'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2025

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Journal articles on the topic "Protochlorophyllide"

1

Kotzabasis, Kiriakos, and Horst Senger. "Isolation and Characterization of 3 Protochlorophyllides from Pigment Mutant C-2 A′ of Scenedesmus obliquus." Zeitschrift für Naturforschung C 41, no. 11-12 (1986): 1001–3. http://dx.doi.org/10.1515/znc-1986-11-1208.

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Abstract Three Protrochlorophyllides (protochlorophyllide) were separated from mutant C-2 A′ of the green alga Scenedesmus obliquus. They show distinct differences in polarity, absorption and fluorescence characteristics. Until further characteristics are established we have to assume that we found monovinyl protochlorophyllide (MV-protochlorophyllide), divinyl protochlorophyllide (DV-protochlorophyllide) and a third protochlorophyllide with different side groups. - The question whether these protochlorophyllides are intermediates in the same pathway or precursors of chlorophylls a, b and RC I
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Mayasich, Joseph M., Sally A. Mayasich, and Constantin A. Rebeiz. "Response of Corn (Zea mays), Soybean (Glycine max), and Several Weed Species to Dark-Applied Photodynamic Herbicide Modulators." Weed Science 38, no. 1 (1990): 10–15. http://dx.doi.org/10.1017/s0043174500056046.

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The photodynamic herbicidal performance of δ-aminolevulinic acid in combination with four chlorophyll biosynthesis modulators was evaluated under greenhouse conditions, using corn, soybean, and ten weed species. Treatments resulted in accumulation of various amounts of protoporphyrin IX and of monovinyl and divinyl Mg-protoporphyrin IX and protochlorophyllide. Accumulation of these tetrapyrroles was accompanied by various degrees of photodynamic injury, depending on treatment, plant species, and somewhat the modulator. The lower photodynamic susceptibility of dark monovinyl/light monovinyl and
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SUN, Wenli, Mohamad H. SHAHRAJABIAN, and Qi CHENG. "The roles of a light-dependent protochlorophyllide oxidoreductase (LPOR), and ATP-dependent dark operative protochlorophyllide oxidoreductase (DPOR) in chlorophyll biosynthesis." Notulae Botanicae Horti Agrobotanici Cluj-Napoca 49, no. 3 (2021): 12456. http://dx.doi.org/10.15835/nbha49312456.

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Chlorophyll is a green photosynthetic pigment, and photosynthesis drives the global carbon cycle. The reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate stage of biosynthesis of chlorophyll (Chl) is catalyzed by light-independent protochlorophyllide reducatse (DPOR), and the light-dependent protochlorophyllide oxidoreductase (LPOR). The search was done to all manuscript sections according to terms chlorophyll, a light-dependent protochlorophyllide oxidoreductase, ATP-dependent dark operative protochlorophyllide oxidoreductase, chlorophyll, photosynthesis a
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Nayar, Parmesh, and Tadhg P. Begley. "Protochlorophyllide Reductase III: Synthesis of a Protochlorophyllide-Dihydroflavin Complex." Photochemistry and Photobiology 63, no. 1 (1996): 100–105. http://dx.doi.org/10.1111/j.1751-1097.1996.tb02998.x.

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Kittsteiner, Ursula, Harald Paulsen, Rudolf Schendel, and Wolfhart Rüdiger. "Lack of Light Regulation of NADPH: Protochlorophyllide Oxido-Reductase mRNA in Cress Seedlings (Lepidium sativum L.)." Zeitschrift für Naturforschung C 45, no. 9-10 (1990): 1077–79. http://dx.doi.org/10.1515/znc-1990-9-1024.

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Abstract A cDNA clone for NADPH: protochlorophyllide oxi­doreductase from barley was subcloned for production of antisense-mRNA. This enabled heterologous hybridi­ zation with RNA from cress seedlings (Lepidium sativum L.). The m RNA level for NADPH: protochlorophyllide oxidoreductase did not decrease in cress seedlings during irradiation with continuous far-red or white light up to 12 h. The amount of NADPH: protochlorophyllide oxi­ doreductase protein, identified by Western blot de­ creased 5-fold after continuous irradiation with white light for 12 h. Species differences for light regulatio
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Reza Amirj, Mohammad. "Protochlorophyllide Spectral Forms." Pakistan Journal of Biological Sciences 13, no. 12 (2010): 563–76. http://dx.doi.org/10.3923/pjbs.2010.563.576.

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Chekunova, Elena M. "THE GENETICS OF CHLOROPHYLL BIOSYNTHESIS: LIGHT-INDEPENDENT AND LIGHT-DEPENDENT PATHWAYS." Ecological genetics 8, no. 3 (2010): 38–51. http://dx.doi.org/10.17816/ecogen8338-51.

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The review summarizes contemporary genetical, molecular biological and biochemical data on the two protochlorophyllide oxidoreductases (POR), enzymes responsible of light-dependent (LPOR) and dark-operative (DPOR) protochlorophyllide reduction. Evolutionary aspects of origin and functioning of these enzymes are also discussed. The main focus of this review will be the genetics of archaic dark chlorophyll biosynthesis.
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Walker, Caroline J., and W. Trevor Griffiths. "Protochlorophyllide reductase: A flavoprotein?" FEBS Letters 239, no. 2 (1988): 259–62. http://dx.doi.org/10.1016/0014-5793(88)80929-3.

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McEwen, Birgitta, and Agneta Lindsten. "Characterization of protochlorophyllide and protochlorophyllide esters in roots of dark-grown plants." Physiologia Plantarum 84, no. 3 (1992): 343–50. http://dx.doi.org/10.1111/j.1399-3054.1992.tb04674.x.

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Ewen, Birgitta Mc, and Agneta Lindsten. "Characterization of protochlorophyllide and protochlorophyllide esters in roots of dark-grown plants." Physiologia Plantarum 84, no. 3 (1992): 343–50. http://dx.doi.org/10.1034/j.1399-3054.1992.840304.x.

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Dissertations / Theses on the topic "Protochlorophyllide"

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Proudfoot, Andrew William. "Structural studies of NADPH : protochlorophyllide oxidoreductase." Thesis, University of Sheffield, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.574533.

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The light driven enzyme Protochlorophyllide Oxidoreductase (POR) is responsible for catalysing the reduction of the Cl7 – C18 double bond of the D ring of protochlorophyllide (Pchlide), in the presence of NADPH, forming chlorophyllide (Chlide). The reduction of Pchlide involves a light-induced hydride transfer reaction from the pro-S face of nicotinamide adenine dinucleotide phosphate (NADPH) to the C'7 position, coupled to the addition of a proton to the C'8 position forming Chlide. The reaction catalysed by POR is a key step in chlorophyll biosynthesis and is essential in the development of
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Walker, C. J. "The photoreduction of protochlorophyllide and greening." Thesis, University of Bristol, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.375393.

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Kay, S. A. "Photoregulation of the levels of protochlorophyllide reductase." Thesis, University of Bristol, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.354460.

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Townley, Helen Elizabeth. "The purification and molecular characterization of protochlorophyllide oxidoreductase." Thesis, University of Bristol, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.246265.

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Soffe, Mark S. "ATP Usage in the Dark-Operative Protochlorophyllide Oxidoreductase." DigitalCommons@USU, 2016. https://digitalcommons.usu.edu/etd/4753.

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Photosynthesis is a fundamental biological process that sustains life on earth. Chlorophyll is the pigment that captures sunlight and converts it to chemical energy through photosynthesis. These essential light-harvesting compounds are found in photosynthetic plants, cyanobacteria, green algae, angiosperms and gymnosperms. In the chlorophyll biosynthetic pathway, protochlorophyllide (Pchlide) serves as the precursor molecule for chlorophyll. Protochlorophyllide oxidoreductases are a class of enzymes that catalyze the conversion of Pchlide to chlorophyllide a (Chlide), which subsequently is red
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Kovacevic, Dragan. "Phototransformation de la protochlorophyllide en chlorophyllide et les effets des facteurs externes chez des feuilles d'orge étiolées /." Montréal : Université du Québec à Montréal, 2005. http://accesbib.uqam.ca/cgi-bin/bduqam/transit.pl?&noMan=24249680.

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Rowe, Jeremy Dean. "Protochlorophyllide reductase in cyanobacteria and its role in chlorophyll synthesis." Thesis, University of Bristol, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294428.

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Fredericks, Mark Christopher. "Characterisation of the light independent reduction of protochlorophyllide in photosynthetic bacteria." Thesis, University of Bristol, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.390132.

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Hoeven, Robin. "Investigating the contribution of protein dynamics to catalysis in protochlorophyllide oxidoreductase." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/investigating-the-contribution-of-protein-dynamics-to-catalysis-in-protochlorophyllide-oxidoreductase(029dda21-023f-4fdb-a980-26db7eab4833).html.

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Enzyme dynamics has been established to play a crucial role in catalysis, and it has therefore become an important area of research to better understand enzymatic rate enhancements. The light-activated enzyme protochlorophyllide oxidoreductase (POR) is a well-studied model system where dynamics are known to be important for catalysis. The catalytic reaction involves a sequential hydride and proton transfer to reduce the C17-C18 double bond in the protochlorophyllide (Pchlide) substrate with NADPH as a cofactor to yield the chlorophyllide (Chlide) product. Both H-transfer steps are established
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Armstrong, David. "Structural and functional studies of the light-dependent protochlorophyllide oxidoreductase enzyme." Thesis, University of Sheffield, 2014. http://etheses.whiterose.ac.uk/8424/.

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The light dependent enzyme protochlorophyllide oxidoreductase (POR) is a key enzyme in the chlorophyll biosynthesis pathway, catalysing the reduction of the C17 C18 bond in protochlorophyllide (Pchlide) to form chlorophyllide (Chlide). This reaction involves the light-induced transfer of a hydride from the nicotinamide adenine dinucleotide phosphate (NADPH) cofactor, followed by proton transfer from a catalytic tyrosine residue. Much work has been done to elucidate the catalytic mechanism of POR, however little is known about the protein structure. POR isoforms in plants are also notable as co
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Books on the topic "Protochlorophyllide"

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Geiges, Bernd. Regulation der "Protochlorophyllid Oxidoreduktase" Gene A und B aus "Arabidopsis thaliana". Eidgenössische Technische Hochschule Zürich, 2000.

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2

Runge, Sönke. Molekularbiologische und genetische Charakterisierung der NADPH: Protochlorophyllid-Oxidoreduktase während der lichtinduzierten Ergrünung von Arabidopsis thaliana. [s.n.], 1994.

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3

Sironval, C., and M. Brouers. Protochlorophyllide Reduction and Greening. Springer, 2012.

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Sironval, C. Protochlorophyllide Reduction and Greening. Springer, 2011.

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Holtorf, Hauke. Isolation and characterization of a novel NADPH-protochlorophyllide oxidoreductase (PORB) from barley (Hordeum vulgare L.). 1995.

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Schoefs, Benoit, and Benoît Schoefs. Photoreduction of protochlorophyllide "a" to chlorophyllide "a" during the biogenesis of the photosynthetic apparatus in higher plants. Dissertation.com, 2000.

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Sperling, Ulrich. The in vivo functions of NADPH: Protochlorophyllide oxidoreductases A and B as studied by genetic manipulation of their expression in Arabidopsis thaliana. 1998.

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Görschen, Eckart. Untersuchungen zur Transformation und Transkription von sense- und antisense-Konstrukten der NADPH: Protochlorophyllid-Oxidoreduktase-cDNA in Arabidopsis thaliana (L.) Heynh. 1992.

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Book chapters on the topic "Protochlorophyllide"

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Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Protochlorophyllide reductase." In Enzyme Handbook. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_106.

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Adamson, Heather, Caroline Walker, Annette Bees, and Trevor Griffiths. "Protochlorophyllide Reduction in Anabaena." In Progress in Photosynthesis Research. Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-017-0519-6_98.

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Wiktorsson, B., M. Ryberg, and C. Sundqvist. "IEF of Solubilized Active Protochlorophyllide Reductase." In Regulation of Chloroplast Biogenesis. Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3366-5_32.

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Savchenko, G. E., L. M. Abramchik, E. A. Klyuchareva, and M. T. Chaika. "NADPH: Protochlorophyllide Oxidoreductase in Barley (Hordeum Vulgare) Seedlings." In Current Research in Photosynthesis. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_618.

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Moser, Jürgen, and Markus J. Bröcker. "Methods for Nitrogenase-Like Dark Operative Protochlorophyllide Oxidoreductase." In Nitrogen Fixation. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-194-9_9.

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Rebeiz, Constantin A. "The Chl a Carboxylic Biosynthetic Routes: Protochlorophyllide a." In Chlorophyll Biosynthesis and Technological Applications. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7134-5_8.

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Wang, Liangsheng, and Tatjana Kleine. "Singlet Oxygen and Protochlorophyllide Detection in Arabidopsis thaliana." In Methods in Molecular Biology. Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0896-8_5.

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Castelfranco, Paul A., Caroline J. Walker, and Jon D. Weinstein. "Biosynthetic Studies on Chlorophylls: From Protoporphyrin IX to Protochlorophyllide." In Ciba Foundation Symposium 180 - The Biosynthesis of the Tetrapyrrole Pigments. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514535.ch11.

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Seyyedi, M., M. P. Timko, and C. Sundqvist. "Protochlorophyllide and Por in the Lip1 Mutant of Pea." In The Chloroplast: From Molecular Biology to Biotechnology. Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4788-0_33.

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Sundqvist, Christer, Bengt Wiktorsson, Zhong Lin, Bela Böddi, and Margareta Ryberg. "Cross-Linking of NADPH-Protochlorophyllide Oxidoreductase in Isolated Prolamellar Bodies." In Regulation of Chloroplast Biogenesis. Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3366-5_31.

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Conference papers on the topic "Protochlorophyllide"

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Dietzek, Benjamin, Robert Hanf, Michael Schmitt, et al. "Photophysics Of Protochlorophyllide." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482519.

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Heyes, Derren J., C. Neil Hunter, Rienk van Grondelle, and Marie Louise Groot. "Ultrafast enzymatic reaction dynamics in protochlorophyllide-oxidoreductase." In International Conference on Ultrafast Phenomena. OSA, 2002. http://dx.doi.org/10.1364/up.2002.wd38.

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Reports on the topic "Protochlorophyllide"

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Timko, Michael P. Structural domains in NADPH: Protochlorophyllide oxidoreductases involved in catalysis and substrate binding. Final report. Office of Scientific and Technical Information (OSTI), 1999. http://dx.doi.org/10.2172/766046.

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Timko, Michael P. NADPH: Protochlorophyllide Oxidoreductase-Structure, Catalytic Function, and Role in Prolamellar Body Formation and Morphogenesis. Office of Scientific and Technical Information (OSTI), 2013. http://dx.doi.org/10.2172/1061451.

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