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Detalhes Referência

Tipo
Artigos em Revista

Tipo de Documento
Artigo Completo

Título
The Sulfur Oxygenase Reductase from the Mesophilic Bacterium Halothiobacillus neapolitanus Is a Highly Active Thermozyme

Participantes na publicação
A. Veith (Author)
H. M. Botelho (Author)
F. Kindinger (Author)
Cláudio M. Gomes (Author)
Dep. Química e Bioquímica
 BioISI
 A. Kletzin (Author)

Resumo
A biochemical, biophysical, and phylogenetic study of the sulfur oxygenase reductase (SOR) from the mesophilic gammaproteobacterium Halothiobacillus neapolitanus (HnSOR) was performed in order to determine the structural and biochemical properties of the enzyme. SOR proteins from 14 predominantly chemolithoautotrophic bacterial and archaeal species are currently available in public databases. Sequence alignment and phylogenetic analysis showed that they form a coherent protein family. The HnSOR purified from Escherichia coli after heterologous gene expression had a temperature range of activity of 10 to 99°C with an optimum at 80°C (42 U/mg protein). Sulfite, thiosulfate, and hydrogen sulfide were formed at various stoichiometries in a range between pH 5.4 and 11 (optimum pH 8.4). Circular dichroism (CD) spectroscopy and dynamic light scattering showed that the HnSOR adopts secondary and quaternary structures similar to those of the 24-subunit enzyme from the hyperthermophile Acidianus ambivalens (AaSOR). The melting point of the HnSOR was ≈20°C lower than that of the AaSOR, when analyzed with CD-monitored thermal unfolding. Homology modeling showed that the secondary structure elements of single subunits are conserved. Subtle changes in the pores of the outer shell and increased flexibility might contribute to activity at low temperature. We concluded that the thermostability was the result of a rigid protein core together with the stabilizing effect of the 24-subunit hollow sphere.

Data de Submissão/Pedido
2011-11-16
Data de Aceitação
2011-11-21
Data de Publicação
2011-12-02

Instituição
INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA

Suporte
Journal of Bacteriology

Identificadores da Publicação
ISSN - 0021-9193

Editora
American Society for Microbiology

Volume
194
Fascículo
3

Número de Páginas
8
Página Inicial
677
Página Final
685

Identificadores do Documento
DOI - https://doi.org/10.1128/jb.06531-11
URL - http://dx.doi.org/10.1128/jb.06531-11


Exportar referência

APA
A. Veith, H. M. Botelho, F. Kindinger, Cláudio M. Gomes, A. Kletzin, (2011). The Sulfur Oxygenase Reductase from the Mesophilic Bacterium Halothiobacillus neapolitanus Is a Highly Active Thermozyme. Journal of Bacteriology, 194, 677-685. ISSN 0021-9193. eISSN . http://dx.doi.org/10.1128/jb.06531-11

IEEE
A. Veith, H. M. Botelho, F. Kindinger, Cláudio M. Gomes, A. Kletzin, "The Sulfur Oxygenase Reductase from the Mesophilic Bacterium Halothiobacillus neapolitanus Is a Highly Active Thermozyme" in Journal of Bacteriology, vol. 194, pp. 677-685, 2011. 10.1128/jb.06531-11

BIBTEX
@article{39289, author = {A. Veith and H. M. Botelho and F. Kindinger and Cláudio M. Gomes and A. Kletzin}, title = {The Sulfur Oxygenase Reductase from the Mesophilic Bacterium Halothiobacillus neapolitanus Is a Highly Active Thermozyme}, journal = {Journal of Bacteriology}, year = 2011, pages = {677-685}, volume = 194 }