Log in

Relevant bibliographies by topics / Protochlorophyllide / Journal articles

To see the other types of publications on this topic, follow the link: Protochlorophyllide.

Journal articles on the topic 'Protochlorophyllide'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Protochlorophyllide.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Wang, Yi-Ting, Chih-Hui Yang, Keng-Shiang Huang, and Jei-Fu Shaw. "Chlorophyllides: Preparation, Purification, and Application." Biomolecules 11, no. 8 (2021): 1115. http://dx.doi.org/10.3390/biom11081115.

Full text

Abstract:

Chlorophyllides can be found in photosynthetic organisms. Generally, chlorophyllides have a-, b-, c-, d-, and f-type derivatives, and all chlorophyllides have a tetrapyrrole structure with a Mg ion at the center and a fifth isocyclic pentanone. Chlorophyllide a can be synthesized from protochlorophyllide a, divinyl chlorophyllide a, or chlorophyll. In addition, chlorophyllide a can be transformed into chlorophyllide b, chlorophyllide d, or chlorophyllide f. Chlorophyllide c can be synthesized from protochlorophyllide a or divinyl protochlorophyllide a. Chlorophyllides have been extensively use

APA, Harvard, Vancouver, ISO, and other styles

12

Reinbothe, C., K. Apel, and S. Reinbothe. "A light-induced protease from barley plastids degrades NADPH:protochlorophyllide oxidoreductase complexed with chlorophyllide." Molecular and Cellular Biology 15, no. 11 (1995): 6206–12. http://dx.doi.org/10.1128/mcb.15.11.6206.

Full text

Abstract:

The NADPH:protochlorophyllide oxidoreductase precursor protein (pPorA) of barley (Hordeum vulgare L. cv. Carina), synthesized from a full-length cDNA clone by coupling in vitro transcription and translation, is a catalytically active protein. It converts protochlorophyllide to chlorophyllide in a light- and NADPH-dependent manner. At least the pigment product of catalysis remains tightly bound to the precursor protein. The chlorophyllide-pPorA complex differs markedly from the protochlorophyllide-pPorA complex with respect to sensitivity to attack by a light-induced, nucleus-encoded, and energ

APA, Harvard, Vancouver, ISO, and other styles

13

Seyyedi, Mehdi, Michael P. Timko, and Christer Sundqvist. "Protochlorophyllide, NADPH-protochlorophyllide oxidoreductase, and chlorophyll formation in the lip1 mutant of pea." Physiologia Plantarum 106, no. 3 (1999): 344–54. http://dx.doi.org/10.1034/j.1399-3054.1999.106313.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Schoefs, Benoît, and Fabrice Franck. "Protochlorophyllide Reduction: Mechanisms and Evolution¶." Photochemistry and Photobiology 78, no. 6 (2007): 543–57. http://dx.doi.org/10.1562/0031-8655(2003)0780543prmae2.0.co2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Schoefs, Benoît, and Fabrice Franck. "Protochlorophyllide Reduction: Mechanisms and Evolution¶." Photochemistry and Photobiology 78, no. 6 (2003): 543. http://dx.doi.org/10.1562/0031-8655(2003)078<0543:prmae>2.0.co;2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Urbig, Thomas, Rosemarie K. C. Knaust, Hilmar Schiller, and Horst Sengera. "Kinetic Studies of Protochlorophyllide Reduction in vitro in the Greening Mutant C-2A' of the Unicellular Green Alga Scenedesmus obliquus." Zeitschrift für Naturforschung C 50, no. 11-12 (1995): 775–80. http://dx.doi.org/10.1515/znc-1995-11-1207.

Full text

Abstract:

The NADPH-protochlorophyllide oxidoreductase, an enzyme catalysing the light-driven conversion of protochlorophyllide to chlorophyllide, was studied in the greening mutant C- 2A′ of the unicellular green alga Scenedesmus obliquus. Studies of the enzyme activity in vitro showed strong dependence on the presence of glycerol and the detergent Triton X-100. Prerequisite for the formation of a photoactive enzyme complex is a sufficient preincubation time with the substrates PChlide and NADPH. A continuous assay system, reading the absorbance increase at the wavelength of chlorophyllide, was used to

APA, Harvard, Vancouver, ISO, and other styles

17

Sytina, Olga A., Derren J. Heyes, C. Neil Hunter, and Marie Louise Groot. "Ultrafast catalytic processes and conformational changes in the light-driven enzyme protochlorophyllide oxidoreductase (POR)." Biochemical Society Transactions 37, no. 2 (2009): 387–91. http://dx.doi.org/10.1042/bst0370387.

Full text

Abstract:

The enzyme POR (protochlorophyllide oxidoreductase), from the family of alcohol dehydrogenases, reduces protochlorophyllide into chlorophyllide on the absorption of light. The reduction involves the transfer of two protons and two electrons and is an important regulatory step in the biosynthesis of chlorophyll. In recent years, due to the availability of large quantities of the pure enzyme, much of the catalytic reaction has been unravelled by using a variety of spectroscopic methods, including ultrafast initial events in catalysis. In addition, it has been demonstrated that a light-activated

APA, Harvard, Vancouver, ISO, and other styles

18

Duke, Stephen O., Rex N. Paul, Josea M. Becerril, and John H. Schmidt. "Clomazone Causes Accumulation of Sesquiterpenoids in Cotton (Gossypium hirsutumL.)." Weed Science 39, no. 3 (1991): 339–46. http://dx.doi.org/10.1017/s0043174500073033.

Full text

Abstract:

The herbicide clomazone caused ultrastructural damage to etioplasts of cotton cotyledons. Etioplast envelopes were irregular, prothylakoids were absent or irregular, stroma density was low, and there were abnormal stromal vesicles. Further damage occurred upon exposure to light. Clomazone greatly slowed the conversion of chlorophyllide to chlorophyll in cotton, suggesting that phytol synthesis was affected. Neither synthesis of protochlorophyllide nor phototransformation of protochlorophyllide to chlorophyllide was affected by clomazone. Clomazone completely inhibited carotenoid synthesis with

APA, Harvard, Vancouver, ISO, and other styles

19

Lebedev, Nikolai N., and Ether Dujardin. "Energy Transfer from NADPH to Protochlorophyllide in Isolated Protochlorophyllide Holochrome as Determined by UV-Fluorescence Excitation Spectroscopy at 77 K." Zeitschrift für Naturforschung C 48, no. 3-4 (1993): 402–6. http://dx.doi.org/10.1515/znc-1993-3-447.

Full text

Abstract:

The low -temperature fluorescence excitation analysis of different protochlorophyllide (PChlide) forms has been extended to the UV part of the spectrum . A new band at about 360 nm was detected in excitation spectra of active PChlide forms bound to isolated protochlorophyllide holochrome. This band is very similar to the absorbance of NADPH in this region and its intensity depends on the redox state of the surrounding medium. On illumination at low temperature the intensity of the band decreases considerably with out any corresponding changes in the redox state of “ free” NADPH in the surround

APA, Harvard, Vancouver, ISO, and other styles

20

Whyte, B. J., and W. T. Griffiths. "8-vinyl reduction and chlorophyll a biosynthesis in higher plants." Biochemical Journal 291, no. 3 (1993): 939–44. http://dx.doi.org/10.1042/bj2910939.

Full text

Abstract:

A technique involving solid-phase extractions and polyethylene h.p.l.c. suitable for the routine compositional analysis of the total protochlorophyllide pool of plants is described. The resynthesis kinetics of the individual components of the pool have been studied in briefly illuminated etiolated tissue of wheat (Triticum aestivum) and cucumber (Cucumis sativus) during subsequent redarkening. The data are interpreted in terms of a precursor-product relationship between the di- and mono-vinyl analogues of protochlorophyllide during their reaccumulation in darkness. The interconversion is assum

APA, Harvard, Vancouver, ISO, and other styles

21

Dujardin, E., F. Franck, R. Gysemberg, and C. Sironval. "The protochlorophyllide-chlorophyllide cycle and photosynthesis." Photobiochemistry and Photobiophysics 12, no. 1-2 (1986): 97–105. http://dx.doi.org/10.1016/s0165-8646(24)00358-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Darrah, P. M., S. A. Kay, G. R. Teakle, and W. T. Griffiths. "Cloning and sequencing of protochlorophyllide reductase." Biochemical Journal 265, no. 3 (1990): 789–98. http://dx.doi.org/10.1042/bj2650789.

Full text

Abstract:

Putative protochlorophyllide reductase cDNA clones (252 and 113) were isolated from an etiolated-oat (Avena sativa) cDNA library. These were used to indirectly characterize a further clone, p127, isolated from a lambda-phage gt11 cDNA library. The latter (1.15 kb in length) was sequenced, and the derived amino acid sequence was shown to be remarkably similar to that derived from chemical analysis of a CNBr-cleavage fragment of the purified reductase, p127 codes for more than 95% of the reductase protein.

APA, Harvard, Vancouver, ISO, and other styles

23

Reinbothe, Christiane, Majida El Bakkouri, Frank Buhr, et al. "Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction." Trends in Plant Science 15, no. 11 (2010): 614–24. http://dx.doi.org/10.1016/j.tplants.2010.07.002.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Garrone, Alessio, Nataliya Archipowa, Peter F. Zipfel, Gudrun Hermann, and Benjamin Dietzek. "Plant Protochlorophyllide Oxidoreductases A and B." Journal of Biological Chemistry 290, no. 47 (2015): 28530–39. http://dx.doi.org/10.1074/jbc.m115.663161.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Vedalankar, Pratishtha, and Baishnab C. Tripathy. "Evolution of light-independent protochlorophyllide oxidoreductase." Protoplasma 256, no. 2 (2018): 293–312. http://dx.doi.org/10.1007/s00709-018-1317-y.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Kotzabasis, Kiriakos, Horst Senger, Petra Langlotz, and Hartmut Follmann. "Stimulation of protochlorophyllide oxidoreductase by thioredoxin." Journal of Photochemistry and Photobiology B: Biology 3, no. 3 (1989): 333–39. http://dx.doi.org/10.1016/1011-1344(89)80037-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Dietzek, Benjamin, Stefanie Tschierlei, Gudrun Hermann, et al. "Protochlorophyllide a: A Comprehensive Photophysical Picture." ChemPhysChem 10, no. 1 (2009): 144–50. http://dx.doi.org/10.1002/cphc.200800536.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

MARTIN, Giles E. M., Michael P. TIMKO, and Helen M. WILKS. "Purification and kinetic analysis of pea (Pisum sativum L.) NADPH:protochlorophyllide oxidoreductase expressed as a fusion with maltose-binding protein in Escherichia coli." Biochemical Journal 325, no. 1 (1997): 139–45. http://dx.doi.org/10.1042/bj3250139.

Full text

Abstract:

NADPH:protochlorophyllide oxidoreductase (POR) catalyses the light-dependent reduction of protochlorophyllide to chlorophyllide, a key reaction in the chlorophyll biosynthetic pathway. To facilitate structure–function studies, POR from pea (Pisum sativum L.) has been overexpressed in Escherichia coli as a fusion with maltose-binding protein (MBP) at 5–10% of the total soluble cell protein. The fusion protein (MBP–POR) has been purified to greater than 90% homogeneity by a two-step affinity-purification procedure. This represents the first successful overexpression and purification of a plant P

APA, Harvard, Vancouver, ISO, and other styles

29

Begley, Tadhg P., and Helen Young. "Protochlorophyllide reductase. 1. Determination of the regiochemistry and the stereochemistry of the reduction of protochlorophyllide to chlorophyllide." Journal of the American Chemical Society 111, no. 8 (1989): 3095–96. http://dx.doi.org/10.1021/ja00190a071.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Griffiths, W. Trevor, Thomas McHugh, and Robert E. Blankenship. "The light intensity dependence of protochlorophyllide photoconversion and its significance to the catalytic mechanism of protochlorophyllide reductase." FEBS Letters 398, no. 2-3 (1996): 235–38. http://dx.doi.org/10.1016/s0014-5793(96)01249-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Gabruk, Michal, and Beata Mysliwa-Kurdziel. "The origin, evolution and diversification of multiple isoforms of light-dependent protochlorophyllide oxidoreductase (LPOR): focus on angiosperms." Biochemical Journal 477, no. 12 (2020): 2221–36. http://dx.doi.org/10.1042/bcj20200323.

Full text

Abstract:

Light-dependent protochlorophyllide oxidoreductase (LPOR) catalyzes the reduction of protochlorophyllide to chlorophyllide, which is a key reaction for angiosperm development. Dark operative light-independent protochlorophyllide oxidoreductase (DPOR) is the other enzyme able to catalyze this reaction, however, it is not present in angiosperms. LPOR, which evolved later than DPOR, requires light to trigger the reaction. The ancestors of angiosperms lost DPOR genes and duplicated the LPORs, however, the LPOR evolution in angiosperms has not been yet investigated. In the present study, we built a

APA, Harvard, Vancouver, ISO, and other styles

32

Belyaeva, O. B., and F. F. Litvin. "Mechanisms of phototransformation of protochlorophyllide into chlorophyllide." Biochemistry (Moscow) 79, no. 4 (2014): 337–48. http://dx.doi.org/10.1134/s0006297914040038.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Schoefs, B. "Protochlorophyllide reduction - what is new in 2005?" Photosynthetica 43, no. 3 (2005): 329–43. http://dx.doi.org/10.1007/s11099-005-0056-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Heyes, Derren J., C. Neil Hunter, Ivo H. M. van Stokkum, Rienk van Grondelle, and Marie Louise Groot. "Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase." Nature Structural & Molecular Biology 10, no. 6 (2003): 491–92. http://dx.doi.org/10.1038/nsb929.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Hanf, Robert, Sonja Fey, Benjamin Dietzek, et al. "Protein-Induced Excited-State Dynamics of Protochlorophyllide." Journal of Physical Chemistry A 115, no. 27 (2011): 7873–81. http://dx.doi.org/10.1021/jp2035899.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Myśliwa-Kurdziel, Beata, Mohammad R. Amirjani, Kazimierz Strzałka, and Christer Sundqvist. "Fluorescence Lifetimes of Protochlorophyllide in Plants with Different Proportions of Short-wavelength and Long-wavelength Protochlorophyllide Spectral Forms¶." Photochemistry and Photobiology 78, no. 2 (2007): 205–12. http://dx.doi.org/10.1562/0031-8655(2003)0780205flopip2.0.co2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Myśliwa-Kurdziel, Beata, Mohammad R. Amirjani, Kazimierz Strzałka, and Christer Sundqvist. "Fluorescence Lifetimes of Protochlorophyllide in Plants with Different Proportions of Short-wavelength and Long-wavelength Protochlorophyllide Spectral Forms¶." Photochemistry and Photobiology 78, no. 2 (2003): 205. http://dx.doi.org/10.1562/0031-8655(2003)078<0205:flopip>2.0.co;2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Amirjani, Mohammad R., and Christer Sundqvist. "Regeneration of protochlorophyllide in green and greening leaves of plants with varying proportions of protochlorophyllide forms in darkness." Physiologia Plantarum 121, no. 3 (2004): 377–90. http://dx.doi.org/10.1111/j.1399-3054.2004.00340.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Heyes, D. J., and C. N. Hunter. "Site-directed mutagenesis of Tyr-189 and Lys-193 in NADPH: protochlorophyllide oxidoreductase from Synechocystis." Biochemical Society Transactions 30, no. 4 (2002): 601–4. http://dx.doi.org/10.1042/bst0300601.

Full text

Abstract:

NADPH: protochlorophyllide oxidoreductase (POR) catalyses the light-dependent reduction of protochlorophyllide to chlorophyllide, a key regulatory reaction in the chlorophyll biosynthetic pathway. Sequence comparisons have revealed that POR is a member of the short-chain alcohol dehydrogenase family of enzymes. A tyrosine and a lysine residue are conserved throughout all members of this family, and are proposed to be within the active site. This present study describes how site-directed mutagenesis has been used to change Tyr-189 to Phe and Lys-193 to Arg in the Synechocystis POR enzyme. The m

APA, Harvard, Vancouver, ISO, and other styles

40

Ougham, Helen Joan, Ann Myfanwy Thomas, Barry John Thomas, Geneviève Anne Frick, and Gregory Aleksandr Armstrong. "Both light‐dependent protochlorophyllide oxidoreductase A and protochlorophyllide oxidoreductase B are down‐regulated in the slender mutant of barley." Journal of Experimental Botany 52, no. 360 (2001): 1447–54. http://dx.doi.org/10.1093/jexbot/52.360.1447.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Lebedev, N., and M. P. Timko. "Protochlorophyllide oxidoreductase B-catalyzed protochlorophyllide photoreduction in vitro: Insight into the mechanism of chlorophyll formation in light-adapted plants." Proceedings of the National Academy of Sciences 96, no. 17 (1999): 9954–59. http://dx.doi.org/10.1073/pnas.96.17.9954.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Fong, Anna, and John M. Archibald. "Evolutionary Dynamics of Light-Independent Protochlorophyllide Oxidoreductase Genes in the Secondary Plastids of Cryptophyte Algae." Eukaryotic Cell 7, no. 3 (2008): 550–53. http://dx.doi.org/10.1128/ec.00396-07.

Full text

Abstract:

ABSTRACT Plastid genes encoding light-independent protochlorophyllide oxidoreductase (LIPOR) subunits were isolated from cryptophyte algae, the first example of such genes in plastids of secondary endosymbiotic origin. The presence of functional and nonfunctional copies of LIPOR genes in cryptophytes suggests that light-independent chlorophyll biosynthesis is a nonessential pathway in these organisms.

APA, Harvard, Vancouver, ISO, and other styles

43

Liu, Ruiyuan, Leng Wang, Yue Meng, Fang Li, Haiyu Nie, and Huizhe Lu. "Role of Thylakoid Lipids in Protochlorophyllide Oxidoreductase Activation: Allosteric Mechanism Elucidated by a Computational Study." International Journal of Molecular Sciences 24, no. 1 (2022): 307. http://dx.doi.org/10.3390/ijms24010307.

Full text

Abstract:

Light-dependent protochlorophyllide oxidoreductase (LPOR) is a chlorophyll synthetase that catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) with indispensable roles in regulating photosynthesis processes. A recent study confirmed that thylakoid lipids (TL) were able to allosterically enhance modulator-induced LPOR activation. However, the allosteric modulation mechanism of LPOR by these compounds remains unclear. Herein, we integrated multiple computational approaches to explore the potential cavities in the Arabidopsis thaliana LPOR and an allosteric site ar

APA, Harvard, Vancouver, ISO, and other styles

44

Fujii, Sho, Koichi Kobayashi, Noriko Nagata, Tatsuru Masuda, and Hajime Wada. "Monogalactosyldiacylglycerol Facilitates Synthesis of Photoactive Protochlorophyllide in Etioplasts." Plant Physiology 174, no. 4 (2017): 2183–98. http://dx.doi.org/10.1104/pp.17.00304.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Dong, Chen-Song, Wei-Lun Zhang, Qiao Wang, et al. "Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase." Proceedings of the National Academy of Sciences 117, no. 15 (2020): 8455–61. http://dx.doi.org/10.1073/pnas.1920244117.

Full text

Abstract:

The reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) is the penultimate step of chlorophyll biosynthesis. In oxygenic photosynthetic bacteria, algae, and plants, this reaction can be catalyzed by the light-dependent Pchlide oxidoreductase (LPOR), a member of the short-chain dehydrogenase superfamily sharing a conserved Rossmann fold for NAD(P)H binding and the catalytic activity. Whereas modeling and simulation approaches have been used to study the catalytic mechanism of this light-driven reaction, key details of the LPOR structure remain unclear. We determined the crysta

APA, Harvard, Vancouver, ISO, and other styles

46

Heyes, Derren J., and C. Neil Hunter. "Making light work of enzyme catalysis: protochlorophyllide oxidoreductase." Trends in Biochemical Sciences 30, no. 11 (2005): 642–49. http://dx.doi.org/10.1016/j.tibs.2005.09.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Scheumann, Verena, Harald Klement, Michael Helfrich, Ulrike Oster, Siegrid Schoch, and Wolfhart Rüdiger. "Protochlorophyllide b does not occur in barley etioplasts." FEBS Letters 445, no. 2-3 (1999): 445–48. http://dx.doi.org/10.1016/s0014-5793(99)00169-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Wilson, R. C., and J. B. Cooper. "A Nodulin cDNA with Homology to Protochlorophyllide Reductase." Plant Physiology 104, no. 1 (1994): 289–90. http://dx.doi.org/10.1104/pp.104.1.289.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Kotzabasis, Klriakos, Mathias Senge, Britta Seyfried, and Horst Senger. "AGGREGATION OF MONOVINYL- and DIVINYL-PROTOCHLOROPHYLLIDE IN ORGANICSOLVENTS." Photochemistry and Photobiology 52, no. 1 (1990): 95–101. http://dx.doi.org/10.1111/j.1751-1097.1990.tb01761.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

APEL, Klaus, Hans-Joachim SANTEL, Tom E. REDLINGER, and Heinz FALK. "The Protochlorophyllide Holochrome of Barley (Hordeum vulgare L.)." European Journal of Biochemistry 111, no. 1 (2005): 251–58. http://dx.doi.org/10.1111/j.1432-1033.1980.tb06100.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!