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FEBS Lett. 1999 Oct 22;460(1):6-10.

Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16.

Author information

1
Institut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Germany. rainer.cramm@rz.hu-berlin.de

Abstract

Nitric oxide (NO) reductase was purified from Ralstonia eutropha (formerly Alcaligenes eutrophus) using a two step chromatographic procedure. Unlike the common NO reductases, the enzyme consists of a single subunit of 75 kDa which contains both high-spin and low-spin heme b, but lacks heme c. One additional iron atom, probably a ferric non-heme iron, was identified per enzyme molecule. Whereas reduced cytochrome c was ineffective as electron donor, NO was reduced at a specific activity of 2.3 micromol/min per mg of protein in the presence of 2-methyl-1,4-naphthoquinol.

PMID:
10571051
DOI:
10.1016/s0014-5793(99)01315-0
[Indexed for MEDLINE]
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