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Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties.

Abstract：

:Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum contains four covalently bound heme c groups/55 kDa subunit as determined by atomic absorption spectroscopy and the pyridine Fe(II)-hemochrome technique. Nitrite reductase was isolated from the membrane fraction as a monomer (M(r) 55 +/- 2 kDa) and as a heterooligomeric complex. Both the monomeric and the complex form of the enzyme exhibited a high specific activity, with up to 1050 mumol NO2-min-1 mg-1. The complex was built from four 55 kDa units and contained a 22 kDa c-type cytochrome which was absent in the monomeric form. EPR spectra of the complex displayed a prominent feature at g 4.83 (baseline crossing). This resonance, which was not observed in the spectra of the monomeric nitrite reductase, was assigned to the 22 kDa c-type cytochrome subunit. Identical results were obtained for the enzyme from Wolinella succinogenes which had been reinvestigated for comparison.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Schumacher W,Hole U,Kroneck PM

doi

10.1006/bbrc.1994.2751

subject

Has Abstract

pub_date

1994-11-30 00:00:00

pages

911-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X84727513

journal_volume

205

pub_type

杂志文章

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