A model for the structure of fumarate reductase in the cytoplasmic membrane of escherichia coli

1984 ◽  
Vol 24 (3) ◽  
pp. 207-216 ◽  
Author(s):  
Joel H. Weiner ◽  
Bernard D. Lemire ◽  
Robert W. Jones ◽  
Wayne F. Anderson ◽  
Douglas G. Scraba
Keyword(s):  
Escherichia Coli ◽  
Cytoplasmic Membrane ◽  
Fumarate Reductase

scholarly journals The effects of anions on fumarate reductase isolated from the cytoplasmic membrane of Escherichia coli

1981 ◽  
Vol 199 (3) ◽  
pp. 473-477 ◽  
Author(s):  
J J Robinson ◽  
J H Weiner
Keyword(s):  
Escherichia Coli ◽  
Cytoplasmic Membrane ◽  
Chemical Properties ◽  
Fumarate Reductase ◽  
Maximal Velocity ◽  
Nitrobenzoic Acid ◽  
Thiol Reagent ◽  
Membrane Bound ◽  
Physical And Chemical ◽  
And Chemical Properties

A broad range of anions was shown to stimulate the maximal velocity of purified fumarate reductase isolated from the cytoplasmic membrane of Escherichia coli, while leaving the Km for fumarate unaffected. Reducing agents potentiate the effects of anions on the activity, but have no effect by themselves. Thermal stability, conformation as monitored by circular dichroism and susceptibility to the thiol reagent 5,5′-dithiobis-(2-nitrobenzoic acid) are also altered by anions. The apparent Km for succinate in the reverse reaction (succinate dehydrogenase activity) varies as a function of anion concentration, but the maximal velocity is not affected. The membrane-bound activity is not stimulated by anions and its properties closely resemble those of the purified enzyme in the presence of anions. Thus it appears that anions alter the physical and chemical properties of fumarate reductase, so that it more closely resembles the membrane-bound form.

Molecular properties of fumarate reductase isolated from the cytoplasmic membrane of Escherichia coli

1982 ◽  
Vol 60 (8) ◽  
pp. 811-816 ◽  
Author(s):  
John J. Robinson ◽  
Joel H. Weiner
Keyword(s):  
Escherichia Coli ◽  
Rhodospirillum Rubrum ◽  
Cytoplasmic Membrane ◽  
Reductase Activity ◽  
Sulfhydryl Group ◽  
Fumarate Reductase ◽  
Molar Ratio ◽  
Heart Mitochondrion ◽  
Visible Absorption ◽  
Nitrobenzoic Acid

Fumarate reductase, purified from the cytoplasmic membrane of Escherichia coli, has been cross-linked with the bifunctional reagent dimethylsuberimidate and shown to exist as an αβ dimer of polypeptides of molecular weights 69 000 and 25 000 in a 1:1 molar ratio. The protein has an s20,W of 7.67S and a D20,W of 6.5 × 10−7 cm2/s. The purified enzyme contained 4–5 mol of nonheme iron and 4–5 mol of acid labile sulfur while the visible absorption spectrum showed a broad peak between 400 and 470 nm owing to the presence of an Fe–S centre and 8α[N-3]histidyl FAD. Fumarate reductase activity was readily inhibited by the sulfhydryl reagents 5,5′-dithiobis-(2-nitrobenzoic acid), p-chloromercuribenzoate, and iodoacetamide. Using 5,5′-dithiobis-(2-nitrobenzoic acid) sulfhydryl group modification was followed as a function of enzyme activity. A single cysteine residue was shown to be required for activity and this essential sulfhydryl group was located in the 69 000 dalton subunit. The amino acid composition of E. coli fumarate reductase was similar to the succinate dehydrogenases from beef heart mitochondrion and Rhodospirillum rubrum.

scholarly journals Structure of fumarate reductase on the cytoplasmic membrane of Escherichia coli.

1983 ◽  
Vol 155 (1) ◽  
pp. 391-397 ◽  
Author(s):  
B D Lemire ◽  
J J Robinson ◽  
R D Bradley ◽  
D G Scraba ◽  
J H Weiner
Keyword(s):  
Escherichia Coli ◽  
Cytoplasmic Membrane ◽  
Fumarate Reductase

scholarly journals The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli.

1992 ◽  
Vol 267 (8) ◽  
pp. 5339-5345
Author(s):  
B Traxler ◽  
C Lee ◽  
D Boyd ◽  
J Beckwith
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Cytoplasmic Membrane

Interaction of Gram-Negative Bacteria with the Lysosomal Fraction of Polymorphonuclear Leukocytes II. Changes in the Cell Envelope of Escherichia coli

1970 ◽  
Vol 1 (3) ◽  
pp. 311-318
Author(s):  
D. Friedberg ◽  
I. Friedberg ◽  
M. Shilo
Keyword(s):  
Escherichia Coli ◽  
Polymorphonuclear Leukocytes ◽  
Cytoplasmic Membrane ◽  
Morphological Changes ◽  
Cell Envelope ◽  
Gram Negative Bacteria ◽  
Intact Cells ◽  
Lysosomal Fraction ◽  
E Coli ◽  
Absorbing Material

Interaction of lysosomal fraction with Escherichia coli caused damage to the cell envelope of these intact cells and to the cytoplasmic membrane of E. coli spheroplasts. The damage to the cytoplasmic membrane was manifested in the release of 260-nm absorbing material and β-galactosidase from the spheroplasts, and by increased permeability of cryptic cells to O -nitrophenyl-β- d -galactopyranoside; damage to the cell wall was measured by release of alkaline phosphatase. Microscope observation showed morphological changes in the cell envelope.

Sign in / Sign up

Export Citation Format

Share Document