A system for the heterologous expression of complex redox proteins in Rhodobacter capsulatus: characterisation of recombinant sulphite : cytochrome c oxidoreductase from Starkeya novella


Autoria(s): Kappler, U.; McEwan, A. G.
Data(s)

01/01/2002

Resumo

The phototrophic purple non-sulfur bacterium Rhodobacter capsulatus expresses a wide variety of complex redox proteins in response to changing environmental conditions. Here we report the construction and evaluation of an expression system for recombinant proteins in that organism which makes use of the dor promoter from the same organism. A generic expression vector, pDorEX, was constructed and used to express sulphite:cytochrome c oxidoreductase from Starkeya novella, a heterodimeric protein containing both molybdenum and haem c. The recombinant protein was secreted to the periplasm and its biochemical properties were very similar to those of the native enzyme. The pDorEX system therefore seems to be potentially useful for heterologous expression of multi-subunit proteins containing complex redox cofactors. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Identificador

http://espace.library.uq.edu.au/view/UQ:62442

Idioma(s)

eng

Publicador

Elsevier Science

Palavras-Chave #Biochemistry & Molecular Biology #Biophysics #Cell Biology #Redox Protein #Molybdoenzyme #Protein Expression #Haem C #Gram-negative Bacteria #Escherichia-coli #Dimethylsulfoxide Reductase #Rhodopseudomonas-capsulata #Sulfite Oxidase #Thiobacillus-novellus #Cloning #Pathway #Operon #Gene #C1 #270804 Genetic Technologies - Transformation, Site-directed Mutagenesis, etc. #780105 Biological sciences
Tipo

Journal Article