Výsledky vyhledávání - "GERD N. LA MAR"

Role of Propionates in Substrate Binding to Heme Oxygenase from Neisseria meningitidis: A Nuclear Magnetic Resonance Study

Autor: Kevin M. Smith, Li-Hua Ma, Gerd N. La Mar, Dungeng Peng, Xuhong Zhang, Michihiko Sato

Publikováno v: Biochemistry. 51:7054-7063

Heme oxygenase (HO) cleaves hemin into biliverdin, iron, and CO. For mammalian HOs, both native hemin propionates are required for substrate binding and activity. The HO from the pathogenic bacterium Neisseria meningitidis (NmHO) possesses a crystall

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b0214518bded1c7c06c29570a65924c
https://doi.org/10.1021/bi3007803

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Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A 1H NMR Study

Autor: Xuhong Zhang, Jerry L. Dallas, Kevin M. Smith, Li-Hua Ma, Michihiko Sato, Dungeng Peng, Gerd N. La Mar, James D. Satterlee

Publikováno v: Biochemistry. 50:8823-8833

Heme oxygenase (HO), from the pathogenic bacterium N. meningitidis(NmHO), which secures host iron, shares many properties with mammalian HOs but also exhibits some key differences. The crystal structure appears more compact, and the crystal-undetecte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4c212d614dfaacf0a3dbf03a451cf0d
https://doi.org/10.1021/bi200978g

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1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure

Autor: Xuhong Zhang, Yangzhong Liu, Gerd N. La Mar, Li-Hua Ma, Tadashi Yoshida

Publikováno v: Journal of Inorganic Biochemistry. 103:10-19

Heme oxygenase carries out stereospecific catabolism of protohemin to yield iron, CO and biliverdin. Instability of the physiological oxy complex has necessitated the use of model ligands, of which cyanide and azide are amenable to solution NMR chara

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0465df32402e52d7ed3b78b1f38a4618
https://doi.org/10.1016/j.jinorgbio.2008.08.012

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Application of the paramagnetic dipole field for solution NMR active site structure determination in low-spin, cyanide-inhibited ferric hemoproteins

Autor: Gerd N. La Mar

Publikováno v: IUBMB Life. 59:513-527

The principles for the application of the paramagnetic dipolar field of low-spin, cyanide-inhibited ferrihemoproteins for determining active site structure are briefly described. The ubiquitous dipolar shifts for assigned residues, together with crys

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::469f43742fd0c40b26e24cd3420993c6
https://doi.org/10.1080/15216540701194121

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1H NMR Study of the Influence of Hemin Vinyl→Methyl Substitution on the Interaction between theC-Terminus and Substrate and the 'Aging' of the Heme Oxygenase fromNeisseria meningitidis: Induction of Active Site Structural Heterogeneity by a Two-Fold Symmetric Hemin

Autor: Yangzhong Liu, James D. Satterlee, Li-Hua Ma, Gerd N. La Mar, Xuhong Zhang, Tadashi Yoshida

Publikováno v: Biochemistry. 45:13875-13888

Solution 1H NMR has been used to characterize the active site molecular and electronic structure of the cyanide-inhibited 2,4-dimethyldeuterohemin complex of the heme oxygenase from Neisseria meningitidis (NmHO) with respect to the mode of interactio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9f059ae85b53e87553af73b95150192d
https://doi.org/10.1021/bi061747q

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Solution 1H NMR Characterization of the Axial Bonding of the Two His in Oxidized Human Cytoglobin

Autor: and Luc Moens, Gerd N. La Mar, Vasyl Bondarenko, Sylvia Dewilde

Publikováno v: Journal of the American Chemical Society

Solution 1H NMR spectroscopy has been used to determine the relative strengths (covalency) of the two axial His-Fe bonds in paramagnetic, S = 1/2, human met-cytoglobin. The sequence specific assignments of crucial portions of the proximal and distal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcb54caebb173fd41c8575da7838fadd
https://doi.org/10.1021/ja063330d

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1H NMR Study of the Magnetic Properties and Electronic Structure of the Hydroxide Complex of Substrate-bound Heme Oxygenase from Neisseria Meningitidis: Influence of the Axial Water Deprotonation on the Distal H-bond Network

Autor: Xuhang Zhang, Yangzhong Liu, Li-Hua Ma, Tadashi Yoshida, Gerd N. La Mar

Publikováno v: Journal of the American Chemical Society. 128:6657-6668

The substrate and active site residues of the low-spin hydroxide complex of the protohemin complex of Neisseria meningitidis heme oxygenase (NmHO) have been assigned by saturation transfer between the hydroxide and previously characterized aquo compl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83505be59e9ba1a7ebf23583931bdcc9
https://doi.org/10.1021/ja0584626

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Modulation of the Axial Water Hydrogen-Bonding Properties by Chemical Modification of the Substrate in Resting State, Substrate-Bound Heme Oxygenase from Neisseria meningitidis; Coupling to the Distal H-Bond Network via Ordered Water Molecules

Autor: Xuhong Zhang, Kevin M. Smith, Tadashi Yoshida, Kevin C. Langry, Li-Hua Ma, Yangzhong Liu, Gerd N. La Mar

Publikováno v: Journal of the American Chemical Society. 128:6391-6399

The hydrogen bonding of ligated water in ferric, high-spin, resting-state substrate complexes of heme oxygenase from Neisseria meningitidis has been systematically perturbed by variable electron-withdrawing substituents on the hemin periphery. The pa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cfda823ad5669b4d8ff817fd3499b02
https://doi.org/10.1021/ja0578505

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1H NMR Investigation of the Solution Structure of Substrate-free Human Heme Oxygenase

Autor: Gerd N. La Mar, Paul R. Ortiz de Montellano, Yiming Li, Karine Auclair, Ray T. Syvitski

Publikováno v: Journal of Biological Chemistry. 279:10195-10205

1H NMR was used to investigate the molecular structure, and dynamic properties of soluble, recombinant, substrate-free human heme oxygenase (apohHO) on a comparative basis with similar studies on the substrate complex. Limited but crucial sequence-sp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::715db3576872e12fa3e88d0dcf730e7a
https://doi.org/10.1074/jbc.m308379200

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