AJ133037.2

Detailed information

Microorganism
Sulfurospirillum deleyianum

Taxonomy
Phylum : Proteobacteria Class : Epsilonproteobacteria Order : Campylobacterales Family : Campylobacteraceae Genus : Sulfurospirillum

Isolation Source
nan

Enzyme Name
Cytochrome c-552

Protein Information
Pro_GenBank I.D： CAB37320.2 Length：516 aa Protein FASTA_sequence: Link

Information about Article
Reference：Schumacher et al., 1994 Title：Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties Pubmed ID：7999130 Pubmed link： Link Full research link： Link 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.

Reference：Schumacher et al., 1994
Title：Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties
Pubmed ID：7999130
Pubmed link： Link
Full research link： Link
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.