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

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

Serum contributions to culture medium: Comparative dehydrogenase activity

Life Sciences ◽  
1969 ◽  
Vol 8 (22) ◽  
pp. 1145-1156 ◽  
Author(s):  
C. De Luca ◽  
A.V. Thomas
Keyword(s):  
Dehydrogenase Activity ◽  
Culture Medium

Oxidation–reduction of methanol, formaldehyde, serine, and formate in Methanosphaera stadtmanae using 14C short- and long-term labelling

1995 ◽  
Vol 41 (11) ◽  
pp. 1048-1053 ◽  
Author(s):  
Z. Lin ◽  
R. Sparling
Keyword(s):  
Dehydrogenase Activity ◽  
Formate Dehydrogenase ◽  
Serine Hydroxymethyltransferase ◽  
Whole Cells ◽  
Cytoplasmic Proteins ◽  
Oxidation Reduction ◽  
Methanosphaera Stadtmanae ◽  
Formaldehyde Oxidation ◽  
Short And Long Term

Methanosphaera stadtmanae derives its energy from the reduction by H2 of CH3OH, but not CO2, indicating there is a block in the CO2 methanogenesis pathway. Both 14CH4 and 14CO2 production were detected in whole cells using [14C]formaldehyde or [14C]serine as substrate. 14CO2 was also observed from [14C]formate in both whole cells and cofactor-depleted cell-free extracts, and NADP-dependent formate dehydrogenase activity was detected. Both formate and serine blocked the formation of 14CO2 from formaldehyde in whole cells. The results confirmed that enzymes involved in the reduction of carbon from the level of methylene-tetrahydromethanopterin in a common methanogenic pathway and a tetrahydromethanopterin-dependent serine hydroxymethyltransferase were present in this organism. However, the production of 14CH4 could not be observed from [14C]formate or 14CO2 plus H2. [14C]Formate was incorporated specifically into histidine and RNA. [14C]Methanol was also found to label rRNA and cytoplasmic proteins, especially corrinoid proteins.Key words: methanogenesis, formate dehydrogenase, formaldehyde oxidation, C1 intermediates.

In vitro requirements for formate dehydrogenase activity from Desulfovibrio

1986 ◽  
Vol 32 (5) ◽  
pp. 425-429 ◽  
Author(s):  
Mary Ann Riederer-Henderson ◽  
Harry D. Peck Jr.
Keyword(s):  
Methylene Blue ◽  
Cytochrome C ◽  
Dehydrogenase Activity ◽  
Electron Acceptor ◽  
Formate Dehydrogenase ◽  
Direct Reduction ◽  
Protein S ◽  
Benzyl Viologen

In Desulfovibrio the protein(s) involved in formate dehydrogenase activity have not been identified or characterized. In situ assays in polyacrylamide gels demonstrated that formate dehydrogenase from either D. gigas or D. vulgaris catalyzed the direct reduction of either methylene blue or benzyl viologen in the presence of formate. Thus, the same protein was active with either electron acceptor. Although the enzyme could be stored in air without irreversible inactivation by O2, activity with either dye was stimulated by the addition of thiols to the assay mixture. In the absence of formate the thiols served as a substrate for the in situ reduction of methylene blue or benzyl viologen by the enzyme. Ammonium sulfate fractionation revealed the presence of a fraction which selectively stimulated activity with either benzyl viologen or cytochrome c3 as the electron acceptor. The stimulating fraction was nondialyzable, heat labile, and unstable upon storage. The fraction from either species could stimulate the formate dehydrogenase activity of the other species. The protein may be of physiological signficance as it increased when the cells were grown on formate, and it stimulated the formate hydrogenlyase system with cytochrome c3 as the electron carrier.

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