A novel kind of multi‐copper protein as terminal oxidoreductase of nitrous oxide respiration in Pseudomonas perfectomarinus

FEBS Letters

Matsubara, Teruo¹  Zumft, Walter G.¹ 

[1] Lehrstuhl für Mikrobiologie, Universität Karlsruhe, Kaiserstr. 12, 7500 Karlsruhe 1, FRG

关键词: Nitrous oxide;    Nitrous oxide reductase;    Copper protein;    Denitrification;    Nitrogen cycle;    Pseudomonas;   

DOI  :  10.1016/0014-5793(82)81253-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown