Výsledky vyhledávání - "Melissa W. Calhoun"

Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems

Autor: Melissa W. Calhoun, Thorsten Friedrich, Hanns Weiss, Yoshihiro Fukumori, Hans Leif, Steven W. Meinhardt, Tomoko Ohnishi, Vladimir D. Sled, Robert B. Gennis

Publikováno v: Journal of Bioenergetics and Biomembranes. 25:347-356

Many bacteria contain proton-translocating membrane-bound NADH-quinone oxidoreductases (NDH-1), which demonstrate significant genetic, spectral, and kinetic similarity with their mitochondrial counterparts. This review is devoted to the comparative a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09ba07d0ccb002eeb4aceec5bebbfcd4
https://doi.org/10.1007/bf00762460

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Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli

Autor: Robert B. Gennis, Melissa W. Calhoun

Publikováno v: Journal of Bacteriology. 175:3013-3019

The nature of the Escherichia coli membrane-bound NADH dehydrogenases and their role in the generation of the proton motive force has been controversial. One E. coli NADH:ubiquinone oxidoreductase has previously been purified to homogeneity, and its

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6feb09f335d215e771df27f3cb44f91
https://doi.org/10.1128/jb.175.10.3013-3019.1993

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Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: Amino acid substitutions for two histidines that are putative CuB ligands

Autor: John J. Hill, Laura Lemieux, Melissa W. Calhoun, Gennis Rb, W J Ingledew, James O. Alben

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

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Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product

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

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Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis

Autor: Laura Lemieux, Melissa W. Calhoun, W J Ingledew, Robert B. Gennis, Jeffrey W. Thomas

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

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The highly conserved methionine of subunit I of the heme-copper oxidases is not at the heme-copper dinuclear center: mutagenesis of M110 in subunit I of cytochrome bo3-type ubiquinol oxidase from Escherichia coli

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

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The cytochrome oxidase superfamily of redox-driven proton pumps

Autor: Jeffrey W. Thomas, Robert B. Gennis, Melissa W. Calhoun

Publikováno v: Trends in biochemical sciences. 19(8)

Most respiratory oxidases of eukaryotic and prokaryotic organisms are members of a superfamily of enzymes that couple the redox energy available from the reduction of molecular oxygen to the mechanism of pumping protons across the membrane. The recen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::317a924545e37d36f84848c8c794001c
https://pubmed.ncbi.nlm.nih.gov/7940677

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Strong-field and integral spin-ligand complexes of the cytochrome bo quinol oxidase in Escherichia coli membrane preparations

Autor: John C. Salerno, Robert B. Gennis, W. John Ingledew, Melissa W. Calhoun

Publikováno v: Biochimica et biophysica acta. 1206(1)

The cytochrome bo -type terminal oxidase of Escherichia coli is an analogue of mammalian aa 3 -type cytochrome c oxidase. The catalytic core of both enzymes is a binuclear site containing a penta-coordinate heme (heme o or a 3 ) and copper (Cu B ). H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::293ab6487556427276dd918ce1d82f63
https://pubmed.ncbi.nlm.nih.gov/8186244

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