Výsledky vyhledávání - "G. N. La Mar"

Elektronická kniha

NMR of Paramagnetic Molecules : Principles and Applications

Autor: G. N. La Mar, W. Dew. Horrocks, R. H. Holm

NMR of Paramagnetic Molecules: Principles and Applications is a compendium of papers that discusses the physical principles behind the technique of nuclear magnetic resonance, as well as, evaluates the scope and limitation of the applications of NMR

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1H and 13C NMR Investigation of the Influence of Nonligated Residue Contacts on the Heme Electronic Structure in Cyanometmyoglobin Complexes Reconstituted with Centro- and Pseudocentrosymmetric Hemins

Autor: G. N. La Mar, Kevin M. Smith, Anh-Tuyet T. Tran, B Hu, Ravindra K. Pandey, Urszula Kolczak, Jon B. Hauksson, Irene N. Rezzano

Publikováno v: Journal of the American Chemical Society. 123:10063-10070

The 1H and 13C chemical shifts for the heme methyls of low-spin, ferric sperm whale cyanometmyoglobin reconstituted with a variety of centrosymmetric and pseudocentrosymmetric hemins have been recorded and analyzed to shed light on the nature of heme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3caf3596ce245e9a534ea70710a2d9d
https://doi.org/10.1021/ja011175r

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Secondary Structure Extensions in Pyrococcus furiosus Ferredoxin Destabilize the Disulfide Bond Relative to That in Other Hyperthermostable Ferredoxins. Global Consequences for the Disulfide Orientational Heterogeneity

Autor: Kara L. Bren, Francis E. Jenney Jr., P. S. Brereton, G. N. La Mar, P. L. Wang, Q. Teng, James B. Howard, M. W. Adams, L. Calzolai

Publikováno v: Biochemistry. 38:8167-8178

The single cubane cluster ferredoxin (Fd) from the hyperthermophilic archaeon Pyrococcus furiosus (Pf) possesses several unique properties when compared even to Fds from other hyperthermophilic archaea or bacteria. These include an equilibrium molecu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::208b8c3213467ea0f903316d84f19bf7
https://doi.org/10.1021/bi990241n

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A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: elucidation of the distal hydrogen bonding network by solution NMR

Autor: Francesca Cutruzzolà, G. N. La Mar, M. Brunori, Wei Zhang, C.T. Allocatelli

Publikováno v: Scopus-Elsevier

The solution 1H NMR structure of the active site and ligand dissociation rate for the cyanomet complex have been determined for a sperm whale myoglobin triple mutant Leu29(B10)-->Tyr, His64(E7)-->Gln, Thr67(E10)-->Arg that mimics the distal residue c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e8d5e78cb75426d2ba17e31195aec0f
https://doi.org/10.1016/s0006-3495(97)78135-9

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Molecular Model of the Solution Structure for the Paramagnetic Four-Iron Ferredoxin from the Hyperthermophilic Archaeon Thermococcus litoralis

Autor: Michael W. W. Adams, A. Donaire, G. N. La Mar, Z. H. Zhou, P. L. Wang

Publikováno v: Biochemistry. 35:11319-11328

A molecular model for the three-dimensional solution structure of the paramagnetic, four-iron ferredoxin (Fd) from the hyperthermophilic archaeon Thermococcus litoralis (Tl) has been constructed on the basis of the reported 1H NMR spectral parameters

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e26dbf531db12f675f3c5c0e5fbebd2f
https://doi.org/10.1021/bi960783u

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1H NMR Investigation of the Paramagnetic Cluster Environment in Pyrococcus furiosus Three-Iron Ferredoxin: Sequence-Specific Assignment of Ligated Cysteines Independent of Tertiary Structure

Autor: G. N. La Mar, Zhi Hao Zhou, Carol M. Gorst, Luigi Calzolai, Michael W. W. Adams, Quincy Teng, You-Hsing Yeh

Publikováno v: Biochemistry. 34:600-610

One- and two-dimensional 1H NMR data tailored to detect paramagnetically relaxed protons near the S = 1/2, three-iron-sulfur cluster of the ferredoxin from the hyperthermophile Pyrococcus furiosus are analyzed to sequence specifically assign the hype

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c28c1f8ef8123ec69fefdb8af048927
https://doi.org/10.1021/bi00002a027

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1H NMR investigation of distal mutant deoxy myoglobins. Interpretation of proximal His contact shifts in terms of a localized distal water molecule

Autor: Masao Ikeda-Saito, M. L. Chiu, F. Dalichow, G. N. La Mar, Stephen G. Sligar, Xuefeng Zhao, Yi Dou

Publikováno v: Journal of Biological Chemistry. 269:29629-29635

1H NMR spectra of a series of distal point mutants of human and sperm whale deoxy myoglobin have been recorded and their spectral parameters compared with those of wild type. The substitutions investigated include His64(E7)-->Gly, Ala, Val, Leu, Ile,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::55caff7d8c7ce479928e015213970874
https://doi.org/10.1016/s0021-9258(18)43927-0

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Proton NMR Investigation of Substrate-Bound Heme Oxygenase: Evidence for Electronic and Steric Contributions to Stereoselective Heme Cleavage

Autor: G Hernández, G. N. La Mar, P R Ortiz de Montellano, Kevin M. Smith, Roberto Paolesse, A Wilks

Publikováno v: Biochemistry. 33:6631-6641

The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge cleavage of hemin to yield biliverdin IX alpha, has been investigated by 1H NMR in both its primarily high-spin and its cyanide-inhibited

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2409ca9a6e8d98ebc3148af682abe72e
https://doi.org/10.1021/bi00187a033

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1H NMR study of the dynamics of the pH modulation of axial coordination in Aplysia limacina (Val(E7)) and sperm whale double mutant His(E7)–>Val,Thr(E10)–>Arg metmyoglobin

Autor: M. Brunori, G. N. La Mar, Francesca Cutruzzolà, P. Ascenzi, Usha Pande, F. Ascoli, C. Travaglini-Allocatelli, Jun Qin

Publikováno v: Journal of Biological Chemistry. 268:24012-24021

The molecular and electronic structure, thermodynamics, dynamics, and mechanism of interconversion of the pH-modulated reversible equilibria of Aplysia limacina metmyoglobin, (metMb), have been investigated by 1H NMR spectroscopy. The four identified

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f3d6f48574e2071869a1ff2ae8b48369
https://doi.org/10.1016/s0021-9258(20)80486-4

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1H NMR investigation of the heme cavity of elephant (E7 Gln) met-cyano-myoglobin. Evidence for a B-helix phenylalanine interaction with bound ligand

Autor: K. Vyas, G. N. La Mar, Ramaswamy Krishnamoorthi, S.D. Emerson, Liping Yu, H Mizukami, Krishnakumar Rajarathnam

Publikováno v: Journal of Biological Chemistry. 268:14826-14835

A combination of one- and two-dimensional NMR experiments has been used to identify and spatially locate the heme pocket residues in the paramagnetic, low spin, met-cyano complex of elephant myoglobin. In addition to assigning resonances of the conse

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4c81dea7da3c157963028e7e02373bb0
https://doi.org/10.1016/s0021-9258(18)82408-5

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