Výsledky vyhledávání - "Mary M. J. Tecklenburg"

Vibrational characterization of azobenzenes, azoxybenzenes and azoaromatic and azoxyaromatic polyethers

Autor: Dillip K Mohanty, Mary M. J. Tecklenburg, Derek J. Kosnak, A Bhatnagar

Publikováno v: Journal of Raman Spectroscopy. 28:755-763

Raman and infrared spectra of a bisphenol-A-containing azoaromatic polyether, a bisphenol-A-containing azoxyaromatic polyether and a bisphenol-A-containing 2-hydroxyazoaromatic polyether were analyzed. Vibrational spectra were also collected for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::eaef85e5110c33d43c42dfbde265757c
https://doi.org/10.1002/(sici)1097-4555(199710)28:10<755::aid-jrs143>3.0.co

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Crystallinity and compositional changes in carbonated apatites: Evidence from

Autor: John-David P, McElderry, Peizhi, Zhu, Kamal H, Mroue, Jiadi, Xu, Barbara, Pavan, Ming, Fang, Guisheng, Zhao, Erin, McNerny, David H, Kohn, Renny T, Franceschi, Mark M Banaszak, Holl, Mary M J, Tecklenburg, Ayyalusamy, Ramamoorthy, Michael D, Morris

Publikováno v: Journal of solid state chemistry. 206

Solid-state (magic-angle spinning) NMR spectroscopy is a useful tool for obtaining structural information on bone organic and mineral components and synthetic model minerals at the atomic-level. Raman and 31P NMR spectral parameters were investigated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a37d6660a72c309861874cdcd3d67c56
https://pubmed.ncbi.nlm.nih.gov/24273344

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Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. Purification, kinetics, proton pumping, and spectral analysis

Autor: Mary M. J. Tecklenburg, Matthew P. Espe, C Lerma, Shelagh Ferguson-Miller, John Fetter, Jonathan P. Hosler

Publikováno v: Journal of Biological Chemistry. 267:24264-24272

Aerobically grown Rhodobacter sphaeroides synthesizes a respiratory chain similar to that of eukaryotes. We describe the purification of the aa3-type cytochrome c oxidase of Rb. sphaeroides as a highly active (Vmax > or = 1800 s-1), three-subunit enz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9773344b710c95437b51fa94035f4c22
https://doi.org/10.1016/s0021-9258(18)35760-0

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Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center

Autor: Younkyoo Kim, James P. Shapleigh, Jonathan P. Hosler, Robert B. Gennis, Mary M. J. Tecklenburg, Gerald T. Babcock, Shelagh Ferguson-Miller

Publikováno v: Proceedings of the National Academy of Sciences. 89:4786-4790

The three-subunit aa3-type cytochrome c oxidase (EC 1.9.3.1) of Rhodobacter sphaeroides is structurally and functionally homologous to the more complex mitochondrial oxidase. The largest subunit, subunit I, is highly conserved and predicted to contai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fe4fbd1ba8f21680e3bc1b38dd2118e
https://doi.org/10.1073/pnas.89.11.4786

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Bone chemical structure response to mechanical stress studied by high pressure Raman spectroscopy

Autor: Michael D. Morris, M. K. Davis, D. H. Kohan, O. de Carmejane, Rupak M. Rajachar, Mary M. J. Tecklenburg, Lars Stixrude

Publikováno v: Calcified tissue international. 76(3)

While the biomechanical properties of bone are reasonably well understood at many levels of structural hierarchy, surprisingly little is known about the response of bone to loading at the ultrastructural and crystal lattice levels. In this study, our

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18378ce668faa0d363cce5309d801f4a
https://pubmed.ncbi.nlm.nih.gov/15742234

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Highly ordered interstitial water observed in bone by nuclear magnetic resonance

Autor: David H. Kohn, Mary M. J. Tecklenburg, Ayorinde Awonusi, Michael D. Morris, Erin E. Wilson, Larry W. Beck

Publikováno v: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research. 20(4)

NMR was used to study the nanostructure of bone tissue. Distance measurements show that the first water layer at the surface of the mineral in cortical bone is structured. This water may serve to couple the mineral to the organic matrix and may play

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbc90f189a4ac574ebb05b6b96d333c3
https://pubmed.ncbi.nlm.nih.gov/15765182

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A loop between transmembrane helices IX and X of subunit I of cytochrome c oxidase caps the heme a-heme a3-CuB center

Autor: James O. Alben, Younkyoo Kim, Mary M. J. Tecklenburg, Gerald T. Babcock, John Fetter, Jonathan P. Hosler, Matthew P. Espe, Jeffrey W. Thomas, Gennis Rb, Shelagh Ferguson-Miller, James P. Shapleigh

Publikováno v: Biochemistry. 33(5)

Site-directed mutants were prepared of four consecutive and highly conserved residues (His-411, Asp-412, Thr-413, Tyr-414) of an extramembrane loop that connects putative transmembrane helices IX and X of subunit I of Rhodobacter sphaeroides cytochro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e8785d20cac7afd00a853baa9af2f59
https://pubmed.ncbi.nlm.nih.gov/8110750

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Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides

Autor: James P. Shapleigh, Robert B. Gennis, Jeffrey W. Thomas, John J. Hill, Shelagh Ferguson-Miller, James O. Alben, Melissa W. Calhoun, Mary M. J. Tecklenburg, Gerald T. Babcock, Jonathan P. Hosler

Publikováno v: Biochemistry. 32(40)

Prokaryotic and eukaryotic cytochrome c oxidases and several bacterial ubiquinol oxidases compose a superfamily of heme-copper oxidases. These enzymes are terminal components of aerobic respiratory chains, the principal energy-generating systems of a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6743989512547b48e9e978c9ac9b7d06
https://pubmed.ncbi.nlm.nih.gov/8399240

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Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo

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

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