Structure and function of nitrite reductase containing two type 1 Cu centers.
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Accession number;04A0258625
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| Title;Structure and function of nitrite reductase containing two type 1 Cu centers. |
| Author;
SUZUKI SHIN'ICHIRO
(Osaka Univ., Graduate School of Sci., JPN)
KOBAYASHI MAYUKO
(Osaka Univ., Graduate School of Sci., JPN)
ITO KOUSHI
(Osaka Univ., Graduate School of Sci., JPN)
FUKUI ATSUSHI
(Osaka Univ., Graduate School of Sci., JPN)
KATAOKA KUNISHIGE
(Kanazawa Univ., Faculty of Sci., JPN)
YAMAGUCHI KAZUYA
(Osaka Univ., Graduate School of Sci., JPN)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.18th;NO.;PAGE.86-87(2003)
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| Figure&Table&Reference;FIG.2 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;We have found that Hyphomicrobium denitrificans NIR (HdNIR, ca. 50kDa) shows unique spectroscopic features of the type 1 Cu, compared with those of Achromobacter cycloclastes NIR (AcNIR) and Alcaligenes xylosoxidans NIR (AxNIR): the visible absorption spectrum implies that the enzyme has two kinds of the type 1 Cu. The genetic analysis of HdNIR indicated that the polypeptide is consist of blue copper protein-like domain (ca. 14kDa) containing one type 1 Cu ligand motif (type 1 CuN: His77, Cys114, His119, and Met124) and NIR-like domain (ca. 35kDa) containing one type 1 Cu ligand motif (type 1 CuC: His219, Cys260, His268, and Met273) and one type 2 Cu ligand motif (His224, His259, and His416). The preparation and characterization of the C114A and C260A mutants disclosed that the blue type 1 CuN and the green type 1 CuC shows an axial EPR signal like the type 1 Cu of AxNIR and a rhombic signal like that of AcNIR, respectively. The catalytic activity of C114A HdNIR is larger than that of the recombinant enzyme by a factor of about 1.7, but the C260A mutant shows hardly enzyme activity. (author abst.) |
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