Digitale Medien
Oxford, UK
:
Blackwell Publishing Ltd
FEMS microbiology letters
67 (1990), S. 0
ISSN:
1574-6968
Quelle:
Blackwell Publishing Journal Backfiles 1879-2005
Thema:
Biologie
Notizen:
In Nitrobacter vulgaris strain Ab1 a membrane-bound nitrite reductase was found to be co-purified with the nitrite oxidoreductase, the key enzyme system of nitrite oxidizing cells. The relative molecular weight of the enzyme, estimated by SDS-PAGE, was assumed to be 63 000. The pH optimum was shown to be 6.1 and the Km value for nitrite 263 μM. The IEP was calculated to be at pH 5.5–6.0. The enzyme was inhibited by N,N-diethyldithiocarbaminate (DDC), o-phenanthroline and ethylmaliendiimide. Dithionite-reduced benzyl and methyl viologen, NADH/FMN, and dithionite-reduced horse heart cytochrome c were suitable electron donors for nitrite reduction. The enriched enzyme produced NO as the only end product and showed weak cytochrome c oxidase activity.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1111/j.1574-6968.1990.tb13847.x
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