ChemInform Abstract: CONTRIBUTIONS TO THE CHEMISTRY OF PYRROLE PIGMENTS. PART XXXV: A REGIOSELECTIVE REVERSIBLE ADDITION TO BILATRIENES‐ABC

Falk, H.; Mueller, N.; Schlederer, Thomas

doi:10.1002/chin.198023104

Cited by 2 publications

(4 citation statements)

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“…2). [35, 36] Isomerization about the 9/10 and 10/11 bonds is rarely observed, because the bilin C10 methine bridge has considerable aromatic character. [37]…”

Section: Biosynthesis and Reactivity Of Bilin Chromophoresmentioning

confidence: 99%

“…2). [35, 36, 38, 39] C4 is also susceptible to nucleophilic attack,[40] although it is more sterically hindered than the C10 position. By contrast, C5 and C15 preferentially react with electrophilic reagents, e.g.…”

Section: Biosynthesis and Reactivity Of Bilin Chromophoresmentioning

confidence: 99%

“…[42, 46] Such a linkage at C10 would result in a rubinoid species consistent with the observed blue absorbance. [36, 46] We further established that photoisomerization of this species at reduced temperature resulted in a slight shift of the blue absorbance maximum,[46] followed by generation of a more conjugated tetrapyrrole chromophore that absorbs green light.…”

Section: Cyanobacteriochromes: a Photosensor For Every Colormentioning

confidence: 99%

“…In the B/G photocycle of CBCR Tlr0924 (blue), we propose formation of a second covalent linkage between Cys499 and C10 of the chromophore in the (15Z) state. [46] Such a linkage at C10 would generate a species similar to bilirubin IXα or phycocyanorubin,[29, 36] explaining the blue absorbance of P b S . The (15Z) P b S form can be photoconverted to a (15E) P b L photoproduct which is in thermal equilibrium with the P g form.…”

Section: Figuresmentioning

confidence: 99%

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A Brief History of Phytochromes

2010

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Photosensory proteins enable living things to detect the quantity and quality of their light environment and to transduce that physical signal into biochemical outputs which entrain their metabolism with the ambient light environment. Phytochromes, which photoconvert between red-absorbing Pr and far-red-absorbing Pfr states, have been the most extensively studied of these interesting proteins. Critical regulators of a number of key adaptive processes in higher plants, including photomorphogenesis and shade avoidance, phytochromes are widespread in photosynthetic and nonphotosynthetic bacteria and even in fungi. Cyanobacterial genomes also possess a plethora of more distant relatives of phytochromes known as cyanobacteriochromes (CBCRs). Biochemical characterization of representative CBCRs has demonstrated that this class of photosensors exhibit a broad range of wavelength sensitivities, spanning the entire visible spectrum. Distinct protein-bilin interactions are responsible for this astonishing array of wavelength sensitivities. Despite this spectral diversity, all members of the extended family of phytochrome photosensors appear to share a common photochemical mechanism for light sensing: photoisomerization of the 15/16 double bond of the bilin chromophore.

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“…2). [35, 36] Isomerization about the 9/10 and 10/11 bonds is rarely observed, because the bilin C10 methine bridge has considerable aromatic character. [37]…”

Section: Biosynthesis and Reactivity Of Bilin Chromophoresmentioning

confidence: 99%