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Chemical Compound Review

biliverdin     3-[2-[(Z)-[(5Z)-3-(2- carboxyethyl)-5-[(4...

Synonyms: Oocyan, biliverdine, uteroverdine, AC1NQWXN, CHEMBL455477, ...
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Disease relevance of biliverdin

  • The chromophores were assembled with Agrobacterium phytochrome Agp1, which incorporates BV as natural chromophore [1].

High impact information on biliverdin

  • Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites [2].
  • Like HY1, the HO3 and HO4 proteins have the capacity to synthesize BV from heme [3].
  • In planta, biliverdin IX alpha (BV) is reduced by the plastid-localized, ferredoxin (Fd)-dependent enzyme P Phi B synthase to yield 3Z-P Phi B [4].
  • This inhibition occurred upstream from calcineurin because BV and CO inhibited NFAT activation in response to ET-1 stimulation but not in response to adenoviral expression of a constitutively active calcineurin mutant [5].
  • CONCLUSIONS: Heme oxygenase-1 and its catalytic by-products, BV and CO, constitute a novel antihypertrophic signaling pathway in cardiac myocytes [5].

Biological context of biliverdin

  • A comparison of the spectral properties (P(r) and P(fr) forms) of all the PCB- and BV-containing chromoproteins reveals that the binding site of the cyanobacterial apoprotein is better suited than the plant (oat) phytochrome to noncovalently incorporate the chromophore and to regulate its photochemistry [6].
  • Common bile duct ligation in the last week of pregnancy induced an upregulation of biliverdin-IXalpha reductase in maternal liver but had no effect on fetal liver and placenta [7].
  • Although the redox active compounds that are generated from HO activity (i.e. iron, biliverdin-IXalpha, and bilirubin-IXa) potentially modulate oxidative stress resistance, increasing evidence points to cytoprotective roles for CO [8].

Associations of biliverdin with other chemical compounds

  • Laser flash photolysis (265-nm) of these pigments led to monophotonic photoionization with quantum yields of 0.08 for BR and 0.03 for BV [9].
  • Heme oxygenase (HO) catalyzes the oxidative cleavage of the alpha-mesocarbon of Fe-protoporphyrin-IX yielding equimolar amounts of biliverdin-IXalpha, free divalent iron, and carbon monoxide (CO) [10].

Analytical, diagnostic and therapeutic context of biliverdin

  • Using a coupled apophytochrome assembly assay and HPLC analysis, we examined the ability of the recombinant proteins to catalyze the ferredoxin-dependent reduction of BV to phytobilins [11].
  • The relative abundance of biliverdin-IXalpha reductase mRNA (determined by real-time quantitative RT-PCR) was fetal liver > placenta > maternal liver [7].


  1. Sterically locked synthetic bilin derivatives and phytochrome Agp1 from Agrobacterium tumefaciens form photoinsensitive Pr- and Pfr-like adducts. Inomata, K., Hammam, M.A., Kinoshita, H., Murata, Y., Khawn, H., Noack, S., Michael, N., Lamparter, T. J. Biol. Chem. (2005) [Pubmed]
  2. Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites. Cunningham, O., Dunne, A., Sabido, P., Lightner, D., Mantle, T.J. J. Biol. Chem. (2000) [Pubmed]
  3. Multiple heme oxygenase family members contribute to the biosynthesis of the phytochrome chromophore in Arabidopsis. Emborg, T.J., Walker, J.M., Noh, B., Vierstra, R.D. Plant Physiol. (2006) [Pubmed]
  4. Purification and biochemical properties of phytochromobilin synthase from etiolated oat seedlings. McDowell, M.T., Lagarias, J.C. Plant Physiol. (2001) [Pubmed]
  5. Heme oxygenase-1 inhibition of MAP kinases, calcineurin/NFAT signaling, and hypertrophy in cardiac myocytes. Tongers, J., Fiedler, B., König, D., Kempf, T., Klein, G., Heineke, J., Kraft, T., Gambaryan, S., Lohmann, S.M., Drexler, H., Wollert, K.C. Cardiovasc. Res. (2004) [Pubmed]
  6. Phytochromes with noncovalently bound chromophores: the ability of apophytochromes to direct tetrapyrrole photoisomerization. Jorissen, H.J., Quest, B., Lindner, I., Tandeau de Marsac, N., Gärtner, W. Photochem. Photobiol. (2002) [Pubmed]
  7. Excretion of fetal biliverdin by the rat placenta-maternal liver tandem. Briz, O., Macias, R.I., Perez, M.J., Serrano, M.A., Marin, J.J. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2006) [Pubmed]
  8. Heme oxygenase/carbon monoxide signaling pathways: regulation and functional significance. Ryter, S.W., Otterbein, L.E., Morse, D., Choi, A.M. Mol. Cell. Biochem. (2002) [Pubmed]
  9. The radical ions and photoionization of bile pigments. Land, E.J., Sloper, R.W., Truscott, T.G. Radiat. Res. (1983) [Pubmed]
  10. Heme oxygenase-1: redox regulation and role in the hepatic response to oxidative stress. Bauer, M., Bauer, I. Antioxid. Redox Signal. (2002) [Pubmed]
  11. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Frankenberg, N., Mukougawa, K., Kohchi, T., Lagarias, J.C. Plant Cell (2001) [Pubmed]
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