Singlet oxygen oxidation products of biliverdin IXα dimethyl ester

Dorazio, Sarina J.; Halepas, Steven; Bruhn, Torsten; Fleming, Kathleen M.; Zeller, Mat­thias; Brückner, Christian

doi:10.1016/j.bmc.2015.11.012

Cited by 6 publications

(4 citation statements)

References 29 publications

(17 reference statements)

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“…Biliverdin possesses antioxidant properties in mammals. Structural evidence for a possible reaction mechanism by which biliverdin can act as an antioxidant is given in Dorazio et al 44 Table 2 compares the Raman frequencies of our sample with Raman frequencies published for biliverdin in Hu et al 45 These authors analyzed five biliverdin compounds using FT-Raman and FT-IR and gave the wavenumbers and corresponding assignments of their vibrational modes obtained. With Raman, they used an excitation laser at 1064 nm that is relatively far from our own excitation line at 514.5 nm, but different excitation frequencies can produce a great variation of the resulting Raman spectra.…”

Section: Raman Vibrations Of Biliverdin and Similar Structuresmentioning

confidence: 88%

Raman and Energy Dispersive Spectroscopy (EDS) Analyses of a Microsubstance Adhering to a Fiber of the Turin Shroud

Laude

Fanti

2017

Appl Spectrosc

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The Raman spectrum of a microsubstance, smeared on a fiber coming from the Shroud of Turin, was compared with numerous spectra published for old or modern pigment dyes, whole bloods, dried bloods, red blood cells, albumin, very ancient blood stains, and various "degradation" products of heme. Within the wavenumber measure accuracy, it is shown that all Raman lines detected above background could correspond to vibration frequencies found in biliverdin-derived compounds except a weak line that we tentatively attributed to amide I. Biliverdin is known as an oxidative ring cleavage product of the heme of blood. Energy dispersive spectroscopy (EDS) analysis of the sample confirms an elemental composition fully compatible with this hypothesis. Therefore, it is very likely that this microsubstance contains products of heme including heme/biliverdin-derived compounds and protein traces (amide I). Nevertheless, other measures will be necessary to confirm it. This method of identification, adding EDS to Raman spectrometry can be applied to nondestructive testing (NDT) of many other microsamples.

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Section: Raman Vibrations Of Biliverdin and Similar Structuresmentioning

confidence: 88%

Raman and Energy Dispersive Spectroscopy (EDS) Analyses of a Microsubstance Adhering to a Fiber of the Turin Shroud

Laude

Fanti

2017

Appl Spectrosc

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“…5). Whether the first biliverdin oxidation step actually takes place at the bond indicated or at the adjacent www.nature.com/scientificreports/ double bond, followed by the loss of the meso-carbon, cannot be determined, but direct and circumstantial evidence exist that at least singlet oxygen reacts specifically with the double bond 33,38 . Bilirubin 4 H is a well-studied catabolite of biliverdin 39 , generated through a reductive enzymatic process 40 .…”

Section: Discussionmentioning

confidence: 99%

Expanding the eggshell colour gamut: uroerythrin and bilirubin from tinamou (Tinamidae) eggshells

Hamchand

Hanley

Prum

et al. 2020

Sci Rep

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To date, only two pigments have been identified in avian eggshells: rusty-brown protoporphyrin IX and blue-green biliverdin IXα. Most avian eggshell colours can be produced by a mixture of these two tetrapyrrolic pigments. However, tinamou (Tinamidae) eggshells display colours not easily rationalised by combination of these two pigments alone, suggesting the presence of other pigments. Here, through extraction, derivatization, spectroscopy, chromatography, and mass spectrometry, we identify two novel eggshell pigments: yellow–brown tetrapyrrolic bilirubin from the guacamole-green eggshells of Eudromia elegans, and red–orange tripyrrolic uroerythrin from the purplish-brown eggshells of Nothura maculosa. Both pigments are known porphyrin catabolites and are found in the eggshells in conjunction with biliverdin IXα. A colour mixing model using the new pigments and biliverdin reproduces the respective eggshell colours. These discoveries expand our understanding of how eggshell colour diversity is achieved. We suggest that the ability of these pigments to photo-degrade may have an adaptive value for the tinamous.

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“…Though the exact mechanism is not known, previous reports reveal that biliverdin is a potential antioxidant in the biliverdin/ bilirubin cycle in the presence of biliverdin reductase and helps cytoprotection (53)(54)(55)(56). However, Dorazio et al (57) have recently shown that biliverdin itself may have antioxidant properties, which might be an added advantage for walleyes for survival in their native environment. Schaefer et al (3) have shown that the number and level of sandercyanin in the mucus of blue walleye increases seasonally, in the summer, as solar UV input increases.…”

Section: Crystal Structures Of Apo-and Holo-sandercyanin Reveal Molecmentioning

confidence: 94%

Blue protein with red fluorescence

Ghosh

Ferraro

et al. 2016

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

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The walleye (Sander vitreus) is a golden yellow fish that inhabits the Northern American lakes. The recent sightings of the blue walleye and the correlation of its sighting to possible increased UV radiation have been proposed earlier. The underlying molecular basis of its adaptation to increased UV radiation is the presence of a protein (Sandercyanin)-ligand complex in the mucus of walleyes. Degradation of heme by UV radiation results in the formation of Biliverdin IXα (BLA), the chromophore bound to Sandercyanin. We show that Sandercyanin is a monomeric protein that forms stable homotetramers on addition of BLA to the protein. A structure of the Sandercyanin-BLA complex, purified from the fish mucus, reveals a glycosylated protein with a lipocalin fold. This protein-ligand complex absorbs light in the UV region (λ max of 375 nm) and upon excitation at this wavelength emits in the red region (λ max of 675 nm). Unlike all other known biliverdin-bound fluorescent proteins, the chromophore is noncovalently bound to the protein. We provide here a molecular rationale for the observed spectral properties of Sandercyanin.Sandercyanin | walleye | blue protein | red fluorescent protein | UV radiation

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Singlet oxygen oxidation products of biliverdin IXα dimethyl ester

Cited by 6 publications

References 29 publications

Raman and Energy Dispersive Spectroscopy (EDS) Analyses of a Microsubstance Adhering to a Fiber of the Turin Shroud

Raman and Energy Dispersive Spectroscopy (EDS) Analyses of a Microsubstance Adhering to a Fiber of the Turin Shroud

Expanding the eggshell colour gamut: uroerythrin and bilirubin from tinamou (Tinamidae) eggshells

Blue protein with red fluorescence

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