Literature DB >> 3004498

N-terminal amino acid sequence of cytochrome c-552 from Nitrosomonas europaea.

D J Miller, D J Nicholas.   

Abstract

Nitrosomonas europaea is an ammonia-oxidizing bacterium which contains multiple c-type cytochromes. Few of these components have been assigned physiological roles, but on the basis of molecular weight and redox potential cytochrome c-552 has been considered to be an analogue of the mitochondrial cytochrome-c family of proteins. We present the N-terminal amino acid sequence (47 residues) of cytochrome c-552 and show that this protein is most closely related to the group of small cytochrome-c components from pseudomonads (cytochromes c-551) and is probably evolutionarily distant from the analagous protein (cytochrome c-550) from the nitrite-oxidizing bacterium Nitrobacter agilis.

Entities:  

Mesh:

Substances:

Year:  1986        PMID: 3004498

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  3 in total

1.  Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea.

Authors:  R Timkovich; D Bergmann; D M Arciero; A B Hooper
Journal:  Biophys J       Date:  1998-10       Impact factor: 4.033

2.  Amino acid sequence of cytochrome c-552 from a thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus.

Authors:  Y Sanbongi; M Ishii; Y Igarashi; T Kodama
Journal:  J Bacteriol       Date:  1989-01       Impact factor: 3.490

3.  The amino acid sequence of Nitrosomonas europaea cytochrome c-552.

Authors:  T Fujiwara; T Yamanaka; Y Fukumori
Journal:  Curr Microbiol       Date:  1995-07       Impact factor: 2.188

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.