Protozoan myoglobin from Paramecium caudatum
Native oxymyoglobin (MbO 2 ) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE‐cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbO 2 used as a reference, Paramecium MbO...
Published in: | European Journal of Biochemistry |
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Language: | English |
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Wiley
1990
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crwiley:10.1111/j.1432-1033.1990.tb19303.x 2024-06-02T08:14:52+00:00 Protozoan myoglobin from Paramecium caudatum Its autoxidation reaction and hemichrome formation TSUBAMOTO, Yoshiharu MATSUOKA, Ariki YUSA, Keisuke SHIKAMA, Keiji 1990 http://dx.doi.org/10.1111/j.1432-1033.1990.tb19303.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1990.tb19303.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1990.tb19303.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 193, issue 1, page 55-59 ISSN 0014-2956 1432-1033 journal-article 1990 crwiley https://doi.org/10.1111/j.1432-1033.1990.tb19303.x 2024-05-03T10:56:27Z Native oxymyoglobin (MbO 2 ) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE‐cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbO 2 used as a reference, Paramecium MbO 2 was found to be much more susceptible to autoxidation over a wide range of pH (4–11) in 0.1 M buffer at 25°C. Kinetic analysis has revealed that a proton‐catalyzed displacement of O 2 − from MbO 2 by an entering water molecule can play a dominant role in the autoxidation reaction of Paramecium MbO 2 to metMb, as in the case of sperm whale MbO 2 involving the distal histidine as its catalytic residue. At pH values higher than 9.5, however, Paramecium MbO 2 was found to be oxidized to yield a hemichrome. The spontaneous formation of hemichromes is at variance with the other known myoglobins and is therefore discussed in relation to the unusual amino acid sequence of Paramecium myoglobin having a large number of deletion [Iwaasa, H. et al. (1989) J. Mol. Biol. 208 , 355–358]. Article in Journal/Newspaper Sperm whale Wiley Online Library European Journal of Biochemistry 193 1 55 59 |
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Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
Native oxymyoglobin (MbO 2 ) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE‐cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbO 2 used as a reference, Paramecium MbO 2 was found to be much more susceptible to autoxidation over a wide range of pH (4–11) in 0.1 M buffer at 25°C. Kinetic analysis has revealed that a proton‐catalyzed displacement of O 2 − from MbO 2 by an entering water molecule can play a dominant role in the autoxidation reaction of Paramecium MbO 2 to metMb, as in the case of sperm whale MbO 2 involving the distal histidine as its catalytic residue. At pH values higher than 9.5, however, Paramecium MbO 2 was found to be oxidized to yield a hemichrome. The spontaneous formation of hemichromes is at variance with the other known myoglobins and is therefore discussed in relation to the unusual amino acid sequence of Paramecium myoglobin having a large number of deletion [Iwaasa, H. et al. (1989) J. Mol. Biol. 208 , 355–358]. |
format |
Article in Journal/Newspaper |
author |
TSUBAMOTO, Yoshiharu MATSUOKA, Ariki YUSA, Keisuke SHIKAMA, Keiji |
spellingShingle |
TSUBAMOTO, Yoshiharu MATSUOKA, Ariki YUSA, Keisuke SHIKAMA, Keiji Protozoan myoglobin from Paramecium caudatum |
author_facet |
TSUBAMOTO, Yoshiharu MATSUOKA, Ariki YUSA, Keisuke SHIKAMA, Keiji |
author_sort |
TSUBAMOTO, Yoshiharu |
title |
Protozoan myoglobin from Paramecium caudatum |
title_short |
Protozoan myoglobin from Paramecium caudatum |
title_full |
Protozoan myoglobin from Paramecium caudatum |
title_fullStr |
Protozoan myoglobin from Paramecium caudatum |
title_full_unstemmed |
Protozoan myoglobin from Paramecium caudatum |
title_sort |
protozoan myoglobin from paramecium caudatum |
publisher |
Wiley |
publishDate |
1990 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1990.tb19303.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1990.tb19303.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1990.tb19303.x |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
European Journal of Biochemistry volume 193, issue 1, page 55-59 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1990.tb19303.x |
container_title |
European Journal of Biochemistry |
container_volume |
193 |
container_issue |
1 |
container_start_page |
55 |
op_container_end_page |
59 |
_version_ |
1800738868877590528 |