Purification and characterization of the single‐component nitric oxide reductase from Ralstonia eutropha H16
Open Access
- 22 October 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 460 (1) , 6-10
- https://doi.org/10.1016/s0014-5793(99)01315-0
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 μmol/min per mg of protein in the presence of 2‐methyl‐1,4‐naphthoquinol.Keywords
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