Heterologous expression of the Desulfovibrio gigas [NiFe] hydrogenase in Desulfovibrio fructosovorans MR400. 1998

M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
Unité de Bioénergétique et Ingénierie des Protéines, IBSM, CNRS, 13402 Marseille Cedex 20, France.

The ability of Desulfovibrio fructosovorans MR400 DeltahynABC to express the heterologous cloned [NiFe] hydrogenase of Desulfovibrio gigas was investigated. The [NiFe] hydrogenase operon from D. gigas, hynABCD, was cloned, sequenced, and introduced into D. fructosovorans MR400. A portion of the recombinant heterologous [NiFe] hydrogenase was totally matured, exhibiting catalytic and spectroscopic properties identical to those of the native D. gigas protein. A chimeric operon containing hynAB from D. gigas and hynC from D. fructosovorans placed under the control of the D. fructosovorans hynAp promoter was constructed and expressed in D. fructosovorans MR400. Under these conditions, the same level of activity was obtained as with the D. gigas hydrogenase operon.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009876 Operon In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION. Operons
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003901 Desulfovibrio A genus of gram-negative, anaerobic, rod-shaped bacteria capable of reducing sulfur compounds to hydrogen sulfide. Organisms are isolated from anaerobic mud of fresh and salt water, animal intestines, manure, and feces.
D004578 Electron Spin Resonance Spectroscopy A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING. ENDOR,Electron Nuclear Double Resonance,Electron Paramagnetic Resonance,Paramagnetic Resonance,Electron Spin Resonance,Paramagnetic Resonance, Electron,Resonance, Electron Paramagnetic,Resonance, Electron Spin,Resonance, Paramagnetic
D006864 Hydrogenase An enzyme found in bacteria. It catalyzes the reduction of FERREDOXIN and other substances in the presence of molecular hydrogen and is involved in the electron transport of bacterial photosynthesis. Ferredoxin Hydrogenase,H2-Oxidizing Hydrogenase,Hydrogenlyase,H2 Oxidizing Hydrogenase,Hydrogenase, Ferredoxin,Hydrogenase, H2-Oxidizing
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA

Related Publications

M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
June 1993, Journal of bacteriology,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
June 2003, Biochemical and biophysical research communications,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
September 2004, Journal of the American Chemical Society,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
February 2002, Journal of bacteriology,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
September 1998, Proceedings of the National Academy of Sciences of the United States of America,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
February 1990, European journal of biochemistry,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
January 1987, The Journal of biological chemistry,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
September 1990, Gene,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
August 2002, FEMS microbiology letters,
M Rousset, and V Magro, and N Forget, and B Guigliarelli, and J P Belaich, and E C Hatchikian
May 1978, Biochemical and biophysical research communications,
Copied contents to your clipboard!