Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria

Biochemistry ◽  
1992 ◽  
Vol 31 (48) ◽  
pp. 12132-12140 ◽  
Author(s):  
Sara L. Pealing ◽  
Ann C. Black ◽  
Forbes D. C. Manson ◽  
F. Bruce Ward ◽  
Stephen K. Chapman ◽  
...  
Keyword(s):  
Shewanella Putrefaciens ◽  
Fumarate Reductase ◽  
Gene Encoding ◽  
Flavocytochrome C ◽  
Membrane Bound ◽  
Membrane Bound Enzymes

Flavocytochrome c: A soluble fumarate reductase from Shewanella putrefaciens.

1993 ◽  
Vol 51 (1-2) ◽  
pp. 183
Author(s):  
Sara L Pealing ◽  
Ann C Black ◽  
Myles R Cheesman ◽  
Stephen K Chapman ◽  
F Bruce Ward ◽  
...  
Keyword(s):  
Shewanella Putrefaciens ◽  
Fumarate Reductase ◽  
Flavocytochrome C

Crystallization and preliminary X-ray crystallographic analysis of a periplasmic tetrahaem flavocytochrome c 3 from Shewanella frigidimarina NCIMB400 which has fumarate reductase activity

1999 ◽  
Vol 55 (6) ◽  
pp. 1222-1225 ◽  
Author(s):  
Vicki Bamford ◽  
Paul S. Dobbin ◽  
Sor-cheng Lee ◽  
Ann Reilly ◽  
Anne K. Powell ◽  
...  
Keyword(s):  
Reductase Activity ◽  
Crystallographic Analysis ◽  
Fumarate Reductase ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Mad Phasing ◽  
Shewanella Frigidimarina ◽  
Flavocytochrome C ◽  
Membrane Bound

The fumarate reductase of Escherichia coli and other bacteria is a membrane-bound enzyme consisting of four subunits. A soluble periplasmic 64 kDa tetrahaem flavocytochrome c 3 from Shewanella frigidimarina NCIMB400 which possesses a catalytic fumarate reductase activity has been crystallized. The crystals belong to space group P212121 with unit-cell parameters a = 72.4, b = 110.1, c = 230.2 Å. Assuming a molecular dimer in the asymmetric unit, the crystals contain 65% solvent and, when cryocooled to 100 K, the crystals diffract to at least 3.0 Å resolution. The crystals, however, display an inherent lack of isomorphism and the plausibility of a MAD phasing experiment has therefore been investigated by measuring the iron K absorption edge from a single crystal.

Flavocytochrome C - a novel fumarate reductase from Shewanella putrefaciens

1991 ◽  
Vol 43 (2-3) ◽  
pp. 311 ◽  
Author(s):  
S.L. Pealing ◽  
A.C. Black ◽  
S.K. Chapman ◽  
F.B. Ward ◽  
G.A. Reid
Keyword(s):  
Shewanella Putrefaciens ◽  
Fumarate Reductase ◽  
Flavocytochrome C

Some Aspects of the Polyhexamethyleneguanidine Salts Effect on Cell Cultures

2014 ◽  
Vol 1 (1) ◽  
pp. 62-67 ◽  
Author(s):  
M. Mandygra ◽  
A. Lysytsia
Keyword(s):  
Proliferative Activity ◽  
Cell Monolayer ◽  
Eukaryotic Cell ◽  
Culture Methods ◽  
Cellular Processes ◽  
Negative Effect ◽  
Membrane Bound ◽  
Membrane Bound Enzymes ◽  
Anion Type ◽  
Cell Culture Methods

Aim. To investigate the effect of polyhexamethyleneguanidine (PHMG) to eukaryotic cell culture. Methods. The passaged bovine tracheal cells culture (TCC) and primary culture of chicken embryo fi broblasts (FCE) were used in the experiments. TCC and FCE monolayers were treated with aqueous solutions of PHMG chloride or succinate. The method of PHMG polycation adsorption to the cells’ plasma membrane together with microscopy were applied. Results. The dependence of PHMG effect on the eukaryotic cells on the agent concentration, duration of exposure and the anion type has been fi xed. The PHMG concentration of 10 –5 per cent (0.1 μg/ml) never causes degradation of the previously formed cell monolayer, while the higher concentrations damage it. The conditions of the PHMG chloride and succinate’s negative effect on cell proliferation and inhibition of monolayer formation were determined. The hypothesis that under certain conditions PHMG stimulates the proliferative activity of the cells has been confi rmed. Stimulation may be associated with non-specifi c stress adaptation of cells. In this case, it is due to modifi cations of the cell membrane after PHMG adsorption to it. Conclusions. PHMG polycation binds with the membrane’s phosphoglycerides fi rmly and irreversibly. A portion of the lipids are removed from participation in the normal cellular processes at that. At the same time, the synthesis of new lipids and membrane-bound enzymes is probably accelerated. The phospholip ids’ neogenesis acceleration can stimulate mitosis under certain conditions. The obtained results can be used in the biotechnologies.

scholarly journals Regulation of membrane-bound enzymes of glycosphingolipid biosynthesis

1984 ◽  
Vol 25 (13) ◽  
pp. 1541-1547
Author(s):  
J D Burczak ◽  
R M Soltysiak ◽  
C C Sweeley
Keyword(s):  
Membrane Bound ◽  
Membrane Bound Enzymes ◽  
Glycosphingolipid Biosynthesis
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