Structure of a novel farnesylated bilin from an insect--formation by α-cleavage of heme A of mitochondrial cytochrome c oxidases?
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractBiliproteins are present in almost all forms of life, and many of them play vital roles in photobiology. The bilin ligand of a recently characterized 500-kDa biliprotein from an insect has been isolated and its structure elucidated with chemical and spectroscopic techniques (UV-visible, IR, MS, NMR, and CD). This blue pigment, named CV-bilin, represents a unique high molecular mass derivative of biliverdin IXα, with an unusual 10E-configuration and a molecular mass of 852 Da, corresponding to C48H60N4O10. The high mass of this open-chain tetrapyrrole results from the presence of an epoxi-dihydroxyethylfarnesyl substituent at C-18 and a hydroxymethyl substituent at C-13. This substitution pattern exactly reflects that of heme A of mitochondrial cytochrome c oxidases with a hydroxyethylfarnesyl chain and a formyl group at corresponding positions of the cyclic tetrapyrrole. As no other natural product is known to show these structural features (heme O, the precursor of heme A, has a methyl group at C-13), this bilin is presumed to be derived from heme A by cleavage of the α-methine bridge and oxidative modifications at C-13 and the hydroxyethylfarnesyl chain. Possibly, a bilin structurally related to this insect bilin is also produced in other organisms as a result of mitochondrial turnover or degradation. As CV-bilin in complex with a specific protein is accumulated at the end of larval life, stored in the pupa, and finally transferred to the oocytes, a possible role of the free or protein-bound pigment in egg or embryonic development is discussed.
CitationStructure of a novel farnesylated bilin from an insect--formation by α-cleavage of heme A of mitochondrial cytochrome c oxidases? 2014, 281 (10):2366-76 FEBS J.
JournalThe FEBS journal
The following license files are associated with this item:
- Very high-density lipoprotein and vitellin as carriers of novel biliverdins IXα with a farnesyl side-chain presumably derived from heme A in Spodoptera littoralis.
- Authors: Kayser H, Nimtz M, Ringler P, Müller SA
- Issue date: 2016 Jan
- Farnesyl biliverdins IXα are novel ligands of biliproteins from moths of the Noctuoidea superfamily: A chemosystematic view of the Lepidoptera.
- Authors: Kayser H, Nimtz M
- Issue date: 2016 Nov
- Biglutaminyl-biliverdin IX alpha as a heme degradation product in the dengue fever insect-vector Aedes aegypti.
- Authors: Pereira LO, Oliveira PL, Almeida IC, Paiva-Silva GO
- Issue date: 2007 Jun 12
- Green colouration of cocoons in Antheraea yamamai (Lepidoptera: Saturniidae): light-induced production of blue bilin in the larval haemolymph.
- Authors: Yamada H, Kato Y
- Issue date: 2004 May
- Evaluating the roles of the heme a side chains in cytochrome c oxidase using designed heme proteins.
- Authors: Zhuang J, Reddi AR, Wang Z, Khodaverdian B, Hegg EL, Gibney BR
- Issue date: 2006 Oct 17