An 88 amino acid long C-terminal sequence of human lactotransferrin |
| |
Authors: | M.-H. Metz-Boutigue J. Jollès J. Mazurier G. Spik J. Montreuil P. Jollès |
| |
Affiliation: | 1. Laboratoire des Protéines, Université de Paris V, 45 rue des Saints-Pères, 75270 Paris Cedex 06 France;2. Laboratoire de Chimie Biologique et Laboratoire associé au CNRS, Université des Sciences et Techniques de Lille-I, 59655 Villeneuve d''Ascq Cedex, France |
| |
Abstract: | The terminal oxidoreductase of nitrous oxide respiration in the marine, denitrifying bacterium, Pseudomonas perfectomarinus, was identified as multi-copper protein and purified to electrophoretic homogeneity. The enzyme reduced N2O to N2 with hydrogen, clostridial hydrogenase, and methyl viologen as electron-donating system. The copper content of the reductase corresponded to ~ 8 copper atoms/120 000 Mr. The subunit structure was dimeric with two peptides of equal size. Manganese, iron and zinc were absent, or were not found in stoichiometric amounts. The oxidized chromophore had absorption maxima at 350, 480, 530, 620 and 780 nm; addition of dithionite produced a blue protein form with maxima at 470, 635 and 740 nm. Both forms of the enzyme were paramagnetic. The same copper protein was also isolated from Pseudomonas stutzeri. |
| |
Keywords: | Nitrous oxide Nitrous oxide reductase Copper protein Denitrification Nitrogen cycle |
本文献已被 ScienceDirect 等数据库收录! |
|