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

FEBS Letters

Cramm, Rainer¹  Pohlmann, Anne¹  Friedrich, Bärbel¹ 

[1] Institut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany

关键词: Nitric oxide reductase;    Heme-copper oxidase;    Quinol oxidase;    Denitrification;    Ralstonia eutropha;    NTA;    nitrilotriacetic acid;    PMS;    phenazine methosulfate;    TMPD;    N;    N;    N′;    N′-tetramethyl-p-phenylenediamine;    EPR;    electron paramagnetic resonance;   

DOI  :  10.1016/S0014-5793(99)01315-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown