The effect of oxygen on Chromatographie behavior and properties of nitrous oxide reductase

FEBS Letters

Frunzke, Kurt¹  Coyle, Catherine L.¹  Zumft, Walter G.¹ 

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

关键词: Nitrous oxide reductase;    Copper protein;    Denitrification;    Nitrate respiration;    Pseudomonas;   

DOI  :  10.1016/0014-5793(85)80785-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Nitrous oxide reductase, a high-M _r copper protein, was purified under anaerobic conditions to yield a spectroscopically new species with 3–5-fold increased catalytic activity over the ‘pink’ form of the enzyme obtained thus far. The preparation was homogeneous by chromatographic and electrophoretic criteria and reduced N₂O to N₂. On aerobic gel filtration of a crude extract, the enzymatic activity was slightly shifted from the Cu-protein towards an apparent lower M _r. This effect was not observed under anaerobic conditions, nor was it observed with the purified enzyme on either aerobic or anaerobic chromatography. In crude extracts, oxygen appears to convert the Cu-protein to a lower activity form at the leading edge of a migrating chromatographic zone.

【 授权许可】

Unknown