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The effect of oxygen on Chromatographie behavior and properties of nitrous oxide reductase
Author(s) -
Zumft Walter G.,
Coyle Catherine L.,
Frunzke Kurt
Publication year - 1985
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(85)80785-7
Subject(s) - chemistry , nitrous oxide reductase , size exclusion chromatography , chromatography , anaerobic exercise , yield (engineering) , enzyme , oxygen , nitrous oxide , reductase , catalysis , electrophoresis , biochemistry , organic chemistry , biology , nitrate reductase , physiology , materials science , metallurgy , nitrite reductase
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 N 2 O to N 2 . 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.