Formate Dehydrogenase Activity in Cells and Outer Membrane Blebs of Desulfovibrio gigas

Anaerobe ◽  
1995 ◽  
Vol 1 (3) ◽  
pp. 175-182 ◽  
Author(s):  
Tina S. Haynes ◽  
Dwight J. Klemm ◽  
Joseph J. Ruocco ◽  
Larry L. Barton
Keyword(s):  
Outer Membrane ◽  
Dehydrogenase Activity ◽  
Formate Dehydrogenase ◽  
Desulfovibrio Gigas ◽  
Membrane Blebs ◽  
In Cells

The Effect of the Simultaneous Addition of Molybdenum and Tungsten to the Culture Medium on the Formate Dehydrogenase Activity from Methylobacterium sp. RXM

1998 ◽  
Vol 36 (6) ◽  
pp. 337-340 ◽  
Author(s):  
Francisco M. Gírio ◽  
J. Carlos Roseiro ◽  
A. Isabel Silva
Keyword(s):  
Dehydrogenase Activity ◽  
Culture Medium ◽  
Formate Dehydrogenase ◽  
Simultaneous Addition ◽  
And Tungsten

Assaying CO2 release for determination of formate dehydrogenase activity in entrapment matrices and aqueous-organic two-phase systems

2006 ◽  
Vol 95 (1) ◽  
pp. 199-203 ◽  
Author(s):  
Marion B. Ansorge-Schumacher ◽  
Sonja Steinsiek ◽  
Werner Eberhard ◽  
Nikolaos Keramidas ◽  
Klaus Erkens ◽  
...  
Keyword(s):  
Dehydrogenase Activity ◽  
Formate Dehydrogenase ◽  
Two Phase ◽  
Phase Systems ◽  
Co2 Release

scholarly journals Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas

Structure ◽  
2002 ◽  
Vol 10 (9) ◽  
pp. 1261-1272 ◽  
Author(s):  
Hans Raaijmakers ◽  
Sofia Macieira ◽  
João M Dias ◽  
Susana Teixeira ◽  
Sergey Bursakov ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Gene Sequence ◽  
Formate Dehydrogenase ◽  
Desulfovibrio Gigas

scholarly journals Neisserial Outer Membrane Vesicles Bind the Coinhibitory Receptor Carcinoembryonic Antigen-Related Cellular Adhesion Molecule 1 and Suppress CD4+ T Lymphocyte Function

2007 ◽  
Vol 75 (9) ◽  
pp. 4449-4455 ◽  
Author(s):  
Hannah S. W. Lee ◽  
Ian C. Boulton ◽  
Karen Reddin ◽  
Henry Wong ◽  
Denise Halliwell ◽  
...  
Keyword(s):  
Carcinoembryonic Antigen ◽  
Outer Membrane ◽  
Membrane Vesicles ◽  
Cellular Adhesion ◽  
Outer Membrane Vesicles ◽  
Bacterial Attachment ◽  
Lymphocyte Function ◽  
Cellular Adhesion Molecules ◽  
Cellular Adhesion Molecule ◽  
Membrane Blebs

ABSTRACT Pathogenic Neisseria bacteria naturally liberate outer membrane “blebs,” which are presumed to contribute to pathology, and the detergent-extracted outer membrane vesicles (OMVs) from Neisseria meningitidis are currently employed as meningococcal vaccines in humans. While the composition of these vesicles reflects the bacteria from which they are derived, the functions of many of their constituent proteins remain unexplored. The neisserial colony opacity-associated Opa proteins function as adhesins, the majority of which mediate bacterial attachment to human carcinoembryonic antigen-related cellular adhesion molecules (CEACAMs). Herein, we demonstrate that the Opa proteins within OMV preparations retain the capacity to bind the immunoreceptor tyrosine-based inhibitory motif-containing coinhibitory receptor CEACAM1. When CD4+ T lymphocytes were exposed to OMVs from Opa-expressing bacteria, their activation and proliferation in response to a variety of stimuli were effectively halted. This potent immunosuppressive effect suggests that localized infection will generate a “zone of inhibition” resulting from the diffusion of membrane blebs into the surrounding tissues. Moreover, it demonstrates that OMV-based vaccines must be developed from strains that lack CEACAM1-binding Opa variants.

scholarly journals Increased drug permeability of a stiffened mycobacterial outer membrane in cells lacking MFS transporter Rv1410 and lipoprotein LprG

2019 ◽  
Vol 111 (5) ◽  
pp. 1263-1282 ◽  
Author(s):  
Michael Hohl ◽  
Sille Remm ◽  
Haig A. Eskandarian ◽  
Michael Dal Molin ◽  
Fabian M. Arnold ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Drug Permeability ◽  
Mfs Transporter ◽  
In Cells

Genetic analysis of mutants of Salmonella typhimurium deficient in formate dehydrogenase activity

1973 ◽  
Vol 120 (4) ◽  
pp. 337-340 ◽  
Author(s):  
M. C. Pascal ◽  
F. Casse ◽  
M. Chippaux ◽  
M. Lepelletier
Keyword(s):  
Genetic Analysis ◽  
Salmonella Typhimurium ◽  
Dehydrogenase Activity ◽  
Formate Dehydrogenase

Properties of formate dehydrogenase from Desulfovibrio gigas

1986 ◽  
Vol 32 (5) ◽  
pp. 430-435 ◽  
Author(s):  
Mary Ann Riederer-Henderson ◽  
Harry D. Peck Jr.
Keyword(s):  
Cytochrome C ◽  
Electron Acceptor ◽  
Formate Dehydrogenase ◽  
Specific Activity ◽  
Ph Optimum ◽  
Benzyl Viologen ◽  
Desulfovibrio Gigas ◽  
Diaphorase Activity ◽  
Lag Period ◽  
Molecular Radius

The formate dehydrogenase from extracts of Desulfovibrio gigas was partially purified to a specific activity of 5600 nmol CO2 ∙ min−1 ∙ mg protein−1. Uniquely for a formate dehydrogenase from anaerobes, the enzyme was stable when stored aerobically. Nevertheless, thiols were required in the assay mixture for enzymatic activity. If the enzyme first catalyzed the transfer of electrons from thiols to benzyl viologen (a diaphorase activity), then formate was oxidized rapidly without a lag period. The enzyme had a molecular weight of approximately 240 000, a pH optimum of 7.5–8.0, and a temperature optimum of 56 °C. Activity with cytochrome c3 (molecular radius (Mr) = 13 000) was about twice that with ferredoxin or flavodoxin as the electron acceptor. These results suggest that the formate dehydrogenase from D. gigas can be activated by transferring electrons from thiols to an electron acceptor and uses cytochrome c3 as the natural electron carrier for the oxidation of formate.

A simple assay for formate dehydrogenase activity by gas chromatography–mass spectrometry

1999 ◽  
Vol 855 (1) ◽  
pp. 337-340 ◽  
Author(s):  
T Shiraishi ◽  
E Fukusaki ◽  
S Kajiyama ◽  
A Kobayashi
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Dehydrogenase Activity ◽  
Formate Dehydrogenase ◽  
Gas Chromatography Mass Spectrometry ◽  
Chromatography Mass Spectrometry
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