The reaction between NADPH and mercuric reductase from Pseudomonas aeruginosa.
نویسندگان
چکیده
منابع مشابه
The reaction between NADPH and mercuric reductase from Pseudomonas aeruginosa.
The reaction between the FAD-containing enzyme, mercuric reductase, and its reducing substrate, NADPH, has been studied at 5 degrees C, pH 7.3, by rapid-scan and fixed-wavelength stopped-flow techniques with the aim to characterize reaction intermediates. With an excess of NADPH the spectral changes observed in rapid-scan experiments can be described by a simple kinetic model, A----B----C----D,...
متن کاملThe electron-transfer reaction between azurin and the cytochrome c oxidase from Pseudomonas aeruginosa.
A stopped-flow investigation of the electron-transfer reaction between oxidized azurin and reduced Pseudomonas aeruginosa cytochrome c-551 oxidase and between reduced azurin and oxidized Ps. aeruginosa cytochrome c-551 oxidase was performed. Electrons leave and enter the oxidase molecule via its haem c component, with the oxidation and reduction of the haem d1 occurring by internal electron tra...
متن کاملThe catalytic mechanism of Pseudomonas aeruginosa cd1 nitrite reductase.
The cd1 NiRs (nitrite reductases) are enzymes catalysing the reduction of nitrite to NO (nitric oxide) in the bacterial energy conversion denitrification process. These enzymes contain two distinct redox centres: one covalently bound c-haem, which is reduced by external electron donors, and another peculiar porphyrin, the d1-haem (3,8-dioxo-17-acrylate-porphyrindione), where nitrite is reduced ...
متن کاملPurification and characterization of cytosolic mercuric reductase from Klebsiella pneumoniae
Mercuric reductase, a cytosolic flavoprotein which catalyzes the NADPHdependent reduction of mercuric ion to metallic mercury, has been purified about 82-fold from Klebsiella pneumoniae cells and kinetic properties were investigated. The purification method consisted of rapid (two-step) and straightforward procedure involving dye matrix affinity chromatography. The freshly native protein exhibi...
متن کاملProtein method for investigating mercuric reductase gene expression in aquatic environments.
A colorimetric assay for NADPH-dependent, mercuric ion-specific oxidoreductase activity was developed to facilitate the investigation of mercuric reductase gene expression in polluted aquatic ecosystems. Protein molecules extracted directly from unseeded freshwater and samples seeded with Pseudomonas aeruginosa PU21 (Rip64) were quantitatively assayed for mercuric reductase activity in microtit...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)90760-x