The Structure of Phytochrome: A Picture Is Worth a Thousand Spectra

Rockwell, Nathan C.; Lagarias, J. Clark

doi:10.1105/tpc.105.038513

Cited by 103 publications

(138 citation statements)

References 76 publications

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“…All phytochromes have a covalently attached linear tetrapyrrole (bilin) chromophore that absorbs light in red and far-red region. 5,[16][17][18][19][20][21][22] Three different bilins are used as chromophores: land plant uses phytochromobilin (PÈB), 1 and cyanobacteria use phycocyanobilin (PCB), 23,24 which is also a chromophore of the light-harvesting pigment, phycocyanin, and differs from PÈB only by substitution of the vinyl group at the C18 position with an ethyl group, 1,24,25 whereas other bacteria use biliverdin (BV) (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

Studies on the Structure and Function of Phytochromes as Photoreceptors Based on Synthetic Organic Chemistry

Inomata

2008

Bulletin of the Chemical Society of Japan

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Section: Introductionmentioning

confidence: 99%

Studies on the Structure and Function of Phytochromes as Photoreceptors Based on Synthetic Organic Chemistry

Inomata

2008

Bulletin of the Chemical Society of Japan

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“…In mammals, CO, a gaseous messenger, has antiinflammatory (11) and antiapoptotic (12) effects, and it is clear that BV and its reduced product bilirubin may function as important antioxidants (13)(14)(15)(16). Moreover, in algae, cyanobacteria, and higher plants, BV is a precursor for the synthesis of essential chromophores (17).…”

mentioning

confidence: 99%

A heme-degradation pathway in a blood-sucking insect

Paiva-Silva

Cruz-Oliveira

Nakayasu

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Hematophagous insects are vectors of diseases that affect hundreds of millions of people worldwide. A common physiological event in the life of these insects is the hydrolysis of host hemoglobin in the digestive tract, leading to a massive release of heme, a known prooxidant molecule. Diverse organisms, from bacteria to plants, express the enzyme heme oxygenase, which catalyzes the oxidative degradation of heme to biliverdin (BV) IX, CO, and iron. Here, we show that the kissing bug Rhodnius prolixus, a vector of Chagas' disease, has a unique heme-degradation pathway wherein heme is first modified by addition of two cysteinylglycine residues before cleavage of the porphyrin ring, followed by trimming of the dipeptides. Furthermore, in contrast to most known heme oxygenases, which generate BV IX␣, in this insect, the end product of heme detoxification is a dicysteinyl-BV IX␥. Based on these results, we propose a heme metabolizing pathway that includes the identified intermediates produced during modification and cleavage of the heme porphyrin ring.biliverdin ͉ heme oxygenase ͉ oxidative stress ͉ Rhodnius

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“…[5] In Pflanzen spielt PFB eine Schlüsselrolle als Lichtrezeptor bei der Photoregulierung der Genexpression. [7] Dies ermçglicht die Anpassung der Pflanze an das füri hre Existenz und ihr Überleben unerlässliche Sonnenlicht. [8] In dieser entscheidenden Funktion agiert PFB als Z/E-Photoschalter.…”

unclassified

Von Chlorophyll abstammende gelbe Phyllobiline höherer Pflanzen als umgebungsgesteuerte, chirale Photoschalter

Wurst

Jockusch

et al. 2016

Angewandte Chemie

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The Structure of Phytochrome: A Picture Is Worth a Thousand Spectra

Cited by 103 publications

References 76 publications

Studies on the Structure and Function of Phytochromes as Photoreceptors Based on Synthetic Organic Chemistry

Studies on the Structure and Function of Phytochromes as Photoreceptors Based on Synthetic Organic Chemistry

A heme-degradation pathway in a blood-sucking insect

Von Chlorophyll abstammende gelbe Phyllobiline höherer Pflanzen als umgebungsgesteuerte, chirale Photoschalter

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