The subunit structure of nitrite reductase purified from the denitrifier Achromobacter cycloclastes
The copper-containing nitrite reductase of Achromobacter cycloclastes has been considered to be a homotrimer with three identical subunits both in the crystal and in solution. In this study, however, the enzyme was found to be a heterotrimer consisting of two subunits with molecular masses of 37 kDa...
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Published in | Bioscience, biotechnology, and biochemistry Vol. 63; no. 11; pp. 2020 - 2022 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
Tokyo
Japan Society for Bioscience, Biotechnology, and Agrochemistry
01.11.1999
Japan Society for Bioscience Biotechnology and Agrochemistry Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | The copper-containing nitrite reductase of Achromobacter cycloclastes has been considered to be a homotrimer with three identical subunits both in the crystal and in solution. In this study, however, the enzyme was found to be a heterotrimer consisting of two subunits with molecular masses of 37 kDa and 36.2 kDa, and the 37 kDa subunit was 6 amino acid residues longer than the smaller subunit. Signal-peptide cleavage sites in its N-terminal region are discussed |
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Bibliography: | F60 2000003139 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.63.2020 |