JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rousset, M.
Right arrow Articles by Hatchikian, E. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rousset, M.
Right arrow Articles by Hatchikian, E. C.

Journal of Bacteriology, September 1998, p. 4982-4986, Vol. 180, No. 18
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Heterologous Expression of the Desulfovibrio gigas [NiFe] Hydrogenase in Desulfovibrio fructosovorans MR400

Marc Rousset, Valérie Magro, Nicole Forget, Bruno Guigliarelli, Jean-Pierre Belaich, and E. Claude Hatchikian*

Unité de Bioénergétique et Ingénierie des Protéines, IBSM, CNRS, 13402 Marseille Cedex 20, France

Received 9 February 1998/Accepted 7 July 1998

The ability of Desulfovibrio fructosovorans MR400 Delta hynABC 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.

* Corresponding author. Mailing address: Unité de Bioénergétique et Ingéniérie des Protéines, IBSM, CNRS, 31, Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. Phone: 04 91 16 41 45. Fax: 04 91 16 45 78. E-mail: hatch{at}ibsm.cnrs-mrs.fr.

Journal of Bacteriology, September 1998, p. 4982-4986, Vol. 180, No. 18
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1998 by the American Society for Microbiology. All rights reserved.