| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2051316 | FEBS Letters | 2005 | 5 Pages |
Abstract
The effect of loss of the 34-kDa periplasmic NosX protein on the properties of N2O reductase was investigated with an N2O-respiration negative, double mutant of the paralogous genes nosX and nirX of Paracoccus denitrificans. In spite of absence of whole-cell N2O-reducing activity, the purified reductase was catalytically active, which attributes NosX a physiological role in sustaining the reaction cycle. N2O reductase exhibited the spectroscopic features of CuA and the redox-inert, paramagnetic state, CuZ∗, of the catalytic center. CuZ∗, hitherto considered the result of spontaneous reaction of the reductase with dioxygen, attains cellular significance.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Patrick Wunsch, Heinz Körner, Frank Neese, Rob J.M. van Spanning, Peter M.H. Kroneck, Walter G. Zumft,