Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin
Abstract The complexes of the three BrCN‐cleaved fragments of sperm whale apomyoglobin with hemin were studied by circular dichroism (CD). In native myoglobin, the heme is located in the middle fragment; the isolated peptide (residues 56–131), however, produces little extrinsic Cotton effects by the...
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crwiley:10.1002/bip.360210407 2024-06-02T08:14:53+00:00 Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin Nakano, Minoru Iwamaru, Hiroshi Tobita, Tohru Yang, Jen Tsi 1982 http://dx.doi.org/10.1002/bip.360210407 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.360210407 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.360210407 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biopolymers volume 21, issue 4, page 805-815 ISSN 0006-3525 1097-0282 journal-article 1982 crwiley https://doi.org/10.1002/bip.360210407 2024-05-03T11:09:39Z Abstract The complexes of the three BrCN‐cleaved fragments of sperm whale apomyoglobin with hemin were studied by circular dichroism (CD). In native myoglobin, the heme is located in the middle fragment; the isolated peptide (residues 56–131), however, produces little extrinsic Cotton effects by the addition of hemin, although about four molecules of hemin are bound to this peptide. In marked contrast, the COOH‐terminal peptide (residues 132–153), which binds three hemin molecules, shows strong Cotton effects in the Soret bands and drastically changes its conformation from unordered to highly helical. The Arg‐modified or Lys‐deaminated peptide no longer undergoes conformational changes by the addition of hemin, suggesting that the two propionic acid groups of one hemin molecule interact with the Arg residue and one of the Lys residues, which stabilizes the induced helical conformation. The NH 2 ‐terminal peptide (residues 1–55) binds one hemin molecules, and the helicity of this fragment is slightly enhanced by the addition of hemin. Both the CD and difference absorption spectra indicate that the mode of interaction between the peptides and hemin are different for the three apomyoglobin fragments. Article in Journal/Newspaper Sperm whale Wiley Online Library Biopolymers 21 4 805 815 |
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Open Polar |
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Wiley Online Library |
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English |
description |
Abstract The complexes of the three BrCN‐cleaved fragments of sperm whale apomyoglobin with hemin were studied by circular dichroism (CD). In native myoglobin, the heme is located in the middle fragment; the isolated peptide (residues 56–131), however, produces little extrinsic Cotton effects by the addition of hemin, although about four molecules of hemin are bound to this peptide. In marked contrast, the COOH‐terminal peptide (residues 132–153), which binds three hemin molecules, shows strong Cotton effects in the Soret bands and drastically changes its conformation from unordered to highly helical. The Arg‐modified or Lys‐deaminated peptide no longer undergoes conformational changes by the addition of hemin, suggesting that the two propionic acid groups of one hemin molecule interact with the Arg residue and one of the Lys residues, which stabilizes the induced helical conformation. The NH 2 ‐terminal peptide (residues 1–55) binds one hemin molecules, and the helicity of this fragment is slightly enhanced by the addition of hemin. Both the CD and difference absorption spectra indicate that the mode of interaction between the peptides and hemin are different for the three apomyoglobin fragments. |
format |
Article in Journal/Newspaper |
author |
Nakano, Minoru Iwamaru, Hiroshi Tobita, Tohru Yang, Jen Tsi |
spellingShingle |
Nakano, Minoru Iwamaru, Hiroshi Tobita, Tohru Yang, Jen Tsi Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin |
author_facet |
Nakano, Minoru Iwamaru, Hiroshi Tobita, Tohru Yang, Jen Tsi |
author_sort |
Nakano, Minoru |
title |
Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin |
title_short |
Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin |
title_full |
Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin |
title_fullStr |
Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin |
title_full_unstemmed |
Influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin |
title_sort |
influence of hemin on the conformation of cyanogen bromide‐cleaved peptides of apomyoglobin |
publisher |
Wiley |
publishDate |
1982 |
url |
http://dx.doi.org/10.1002/bip.360210407 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.360210407 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.360210407 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biopolymers volume 21, issue 4, page 805-815 ISSN 0006-3525 1097-0282 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bip.360210407 |
container_title |
Biopolymers |
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21 |
container_issue |
4 |
container_start_page |
805 |
op_container_end_page |
815 |
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1800738893691092992 |