Structure of a novel farnesylated bilin from an insect--formation by α-cleavage of heme A of mitochondrial cytochrome c oxidases?

2.50
Hdl Handle:
http://hdl.handle.net/10033/324143
Title:
Structure of a novel farnesylated bilin from an insect--formation by α-cleavage of heme A of mitochondrial cytochrome c oxidases?
Authors:
Kayser, Hartmut; Wray, Victor; Nimtz, Manfred
Abstract:
Biliproteins 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.
Citation:
Structure 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.
Journal:
The FEBS journal
Issue Date:
May-2014
URI:
http://hdl.handle.net/10033/324143
DOI:
10.1111/febs.12789
PubMed ID:
24655573
Type:
Article
Language:
en
ISSN:
1742-4658
Appears in Collections:
Publications of Dept. Gene Regulation and Differentiation (RDIF)

Full metadata record

DC FieldValue Language
dc.contributor.authorKayser, Hartmuten
dc.contributor.authorWray, Victoren
dc.contributor.authorNimtz, Manfreden
dc.date.accessioned2014-08-04T13:04:45Z-
dc.date.available2014-08-04T13:04:45Z-
dc.date.issued2014-05-
dc.identifier.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.en
dc.identifier.issn1742-4658-
dc.identifier.pmid24655573-
dc.identifier.doi10.1111/febs.12789-
dc.identifier.urihttp://hdl.handle.net/10033/324143-
dc.description.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.en
dc.language.isoenen
dc.rightsArchived with thanks to The FEBS journalen
dc.titleStructure of a novel farnesylated bilin from an insect--formation by α-cleavage of heme A of mitochondrial cytochrome c oxidases?en
dc.typeArticleen
dc.identifier.journalThe FEBS journalen
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