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A novel kind of multi‐copper protein as terminal oxidoreductase of nitrous oxide respiration in Pseudomonas perfectomarinus
Author(s) -
Zumft Walter G.,
Matsubara Teruo
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81253-2
Subject(s) - pseudomonas stutzeri , copper , oxidoreductase , nitrous oxide reductase , chemistry , copper protein , dithionite , nitrite reductase , zinc , inorganic chemistry , paracoccus denitrificans , nuclear chemistry , nitrate reductase , enzyme , biochemistry , bacteria , organic chemistry , biology , genetics
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 N 2 O to N 2 with hydrogen, clostridial hydrogenase, and methyl viologen as electron‐donating system. The copper content of the reductase corresponded to ∼ 8 copper atoms/120 000 M r . 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 .