Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Laura Lemieux"'
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02f4b3b3b114bf467a8fc04b9216a41d
https://doi.org/10.1021/bi00211a038
https://doi.org/10.1021/bi00211a038
Publikováno v:
Biochemistry. 32:11173-11180
Cytochrome bo from Escherichia coli is a ubiquinol oxidase which is a member of the superfamily of heme-copper respiratory oxidases. This superfamily, which includes the eukaryotic cytochrome c oxidases, has in common a bimetallic center consisting o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6d954911d060c4c5ebb1c3f9c237ea1
https://doi.org/10.1021/bi00092a029
https://doi.org/10.1021/bi00092a029
Publikováno v:
Biochemistry. 32:7692-7697
The cytochrome bo ubiquinol oxidase from Escherichia coli is a five-subunit enzyme which is a member of the superfamily of heme-copper respiratory oxidases. Three of the subunits (I, II, and III) are homologous to the three mitochondrial encoded subu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76f7aecd7e9122e7e012fbeab23284a1
https://doi.org/10.1021/bi00081a013
https://doi.org/10.1021/bi00081a013
Publikováno v:
Biochemistry. 32:11524-11529
The bo-type ubiquinol oxidase of Escherichia coli is a member of the superfamily of structurally related heme-copper respiratory oxidases. The members of this family, which also includes the aa3-type cytochrome c oxidases, contain at least two heme p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8645ebc7657406dfc01dfe11470c21a0
https://doi.org/10.1021/bi00094a008
https://doi.org/10.1021/bi00094a008
Autor:
Laura Lemieux, John Walter Hill, Goswitz Vc, Melissa W. Calhoun, Gennis Rb, James O. Alben, J A Garcia-Horsman
Publikováno v:
Biochemistry. 31:11435-11440
Amino acid sequence data have revealed that the bo-type ubiquinol oxidase from Escherichia coli is closely related to the eukaryotic aa3-type cytochrome c oxidases. In the cytochrome c oxidases, the reduction of oxygen to water occurs at a binuclear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::276d273f40d155aa1b04505dd49dda77
https://doi.org/10.1021/bi00161a023
https://doi.org/10.1021/bi00161a023
Publikováno v:
Journal of Biological Chemistry. 267:2105-2113
The cytochrome o complex of Escherichia coli is a ubiquinol oxidase which is the predominant respiratory terminal oxidase when the bacteria are grown under high oxygen tension. The amino acid sequences of three of the subunits of this quinol oxidase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7888cd477a94d00dbcd64ad0e657bd42
https://doi.org/10.1016/s0021-9258(18)46058-9
https://doi.org/10.1016/s0021-9258(18)46058-9
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3c64f93ac173469f7f3ed9e945309926
https://doi.org/10.1016/s0021-9258(19)38574-6
https://doi.org/10.1016/s0021-9258(19)38574-6
Autor:
Robert B. Gennis, J. Arturo Garcia-Horsman, Laura Lemieux, James O. Alben, Melissa W. Calhoun, Jeffrey W. Thomas
Publikováno v:
FEBS letters. 368(3)
A common feature within the heme-copper oxidase superfamily is the dinuclear heme-copper center. Analysis via extended X-ray absorption fine structure (EXAFS) has led to the proposal that sulfur may be bound to CU B , a component of the dinuclear cen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::639389e46665a74d3842b1757fb46619
https://pubmed.ncbi.nlm.nih.gov/7635213
https://pubmed.ncbi.nlm.nih.gov/7635213
Autor:
Laura Lemieux, John Walter Hill, Gerald T. Babcock, Shelagh Ferguson-Miller, Christos D. Georgiou, Jeffrey W. Thomas, John Fetter, Jonathan P. Hosler, Mary M. J. Tecklenburg, Jixiang Ma, Melissa W. Calhoun, James P. Shapleigh, Robert B. Gennis
Publikováno v:
Journal of bioenergetics and biomembranes. 25(2)
Cytochrome aa3 of Rhodobacter sphaeroides and cytochrome bo of E. coli are useful models of the more complex cytochrome c oxidase of eukaryotes, as demonstrated by the genetic, spectroscopic, and functional studies reviewed here. A summary of site-di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b27d0390548686a2035d51f8534934b
https://pubmed.ncbi.nlm.nih.gov/8389745
https://pubmed.ncbi.nlm.nih.gov/8389745
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.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::551b1539517ed19d8d3a2eecf6134fe1
https://pubmed.ncbi.nlm.nih.gov/2168206
https://pubmed.ncbi.nlm.nih.gov/2168206