Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Visala Chepuri"'
Autor:
Robert J. Brooker, E. A. Matzke, Miriam R. Taylor, Visala Chepuri Goswitz, Amy E. Jessen-Marshall
Publikováno v:
Journal of Biological Chemistry. 271:21927-21932
In the lactose permease of Escherichia coli, transmembrane helix 10 has been shown to be functionally important. The structure of this helix has been examined in greater detail in this study. A total of 46 substitution and 8 insertional mutants were
Autor:
Melissa W. Calhoun, Jeffrey W. Thomas, James O. Alben, John J. Hill, Laura Lemieux, Robert B. Gennis, Visala Chepuri Goswitz
Publikováno v:
Biochemistry. 32:13254-13261
The bo-type ubiquinol oxidase of Escherichia coli is a member of the superfamily of heme-copper oxidases which also includes the aa3-type cytochrome c oxidases. The oxygen-binding binuclear center of cytochrome bo is located in subunit I and consists
Autor:
Visala Chepuri, Robert B. Gennis
Publikováno v:
Journal of Biological Chemistry. 265:12978-12986
The cytochrome o terminal oxidase complex is a component of the aerobic respiratory chain of Escherichia coli. This enzyme catalyzes the oxidation of ubiquinol-8 to ubiquinone-8 within the cytoplasmic membrane and the concomitant reduction of O2 to H
Publikováno v:
Journal of Biological Chemistry. 265:11185-11192
The cytochrome o complex is one of two ubiquinol oxidases in the aerobic respiratory system of Escherichia coli. This enzyme catalyzes the two-electron oxidation of ubiquinol-8 which is located in the cytoplasmic membrane, and the four-electron reduc
Publikováno v:
Protein science : a publication of the Protein Society. 4(3)
The uniporter/symporter/antiporter superfamily is an evolutionarily related group of solute transporters. For the entire superfamily, we have used a new predictive program to identify the transmembrane domains. These transmembrane domains were then a
Publikováno v:
Membrane biochemistry. 10(1)
In the present study lactose permease mutants were isolated which recognize the monosaccharide, L-arabinose. Although the wild-type permease exhibits a poor recognition for L-arabinose, seven independent mutants were identified by their ability to gr
Publikováno v:
Biochimica et biophysica acta. 1018(2-3)
The cytochrome o complex is the predominant terminal oxidase in the aerobic respiratory chain of Escherichia coli when the bacteria are grown under conditions of high aeration. The oxidase is a ubiquinol oxidase and reduces molecular oxygen to water.
Publikováno v:
Membrane Biochemistry; 1993, Vol. 10 Issue 1, p61-70, 10p
Publikováno v:
Annals of the New York Academy of Sciences. 550:314-324
Autor:
Goswitz, Visala Chepuri a, Matzke, Elizabeth A. a, Taylor, Miriam R. a, Jessen-Marshall, Amy E. a, Brooker, Robert J. a
Publikováno v:
In Journal of Biological Chemistry 6 September 1996 271(36):21927-21932