A ZnS4Structural Zinc Site in theHelicobacter pyloriFerric Uptake Regulator

Biochemistry ◽  
2009 ◽  
Vol 48 (24) ◽  
pp. 5582-5591 ◽  
Author(s):  
Sylvia Vitale ◽  
Caroline Fauquant ◽  
David Lascoux ◽  
Kristine Schauer ◽  
Christine Saint-Pierre ◽  
...  
Keyword(s):  
Zinc Site

Transportation of Na and Li in Hydrothermally Grown ZnO

2009 ◽  
Vol 1201 ◽  
Author(s):  
Pekka Tapio Neuvonen ◽  
Lasse Vines ◽  
Klaus Magnus Johansen ◽  
Anders Hallén ◽  
Bengt Gunnar Svensson ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Activation Energy ◽  
Formation Energy ◽  
Secondary Ion Mass Spectrometry ◽  
Diffusion Constant ◽  
Zinc Vacancy ◽  
Diffusion Source ◽  
Secondary Ion ◽  
Zinc Site ◽  
Limited Diffusion

AbstractSecondary ion mass spectrometry has been applied to study the transportation of Na and Li in hydrothermally grown ZnO. A dose of 1015 cm-2 of Na+ was implanted into ZnO to act as a diffusion source. A clear trap limited diffusion is observed at temperatures above 550 °C. From these profiles, an activation energy for the transport of Na of ∼1.7 eV has been extracted. The prefactor for the diffusion constant and the solid solubility of Na cannot be deduced independently from the present data but their product estimated to be ∼3 × 1016 cm-1s-1. A dissociation energy of ∼2.4 eV is extracted for the trapped Na. The measured Na and Li profiles show that Li and Na compete for the same traps and interact in a way that Li is depleted from Na-rich regions. This is attributed to a lower formation energy of Na-on-zinc-site than that for Li-on-zinc-site defects and the zinc vacancy is considered as a major trap for migrating Na and Li atoms. Consequently, the diffusivity of Li is difficult to extract accurately from the present data, but in its interstitial configuration Li is indeed highly mobile having a diffusivity in excess of 10-11 cm2s-1 at 500 °C.

Structural characterization of the zinc site in Escherichia coliL-threonine dehydrogenase using extended X-ray absorption fine structure spectroscopy

1998 ◽  
Vol 275-276 ◽  
pp. 215-221 ◽  
Author(s):  
Kimber Clark-Baldwin ◽  
Adam R. Johnson ◽  
Yen-Wen Chen ◽  
Eugene E. Dekker ◽  
James E. Penner-Hahn
Keyword(s):  
Fine Structure ◽  
Structural Characterization ◽  
X Ray ◽  
Threonine Dehydrogenase ◽  
Absorption Fine ◽  
X Ray Absorption ◽  
Zinc Site

Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. Evidence for a dinuclear zinc site

2007 ◽  
Vol 1774 (2) ◽  
pp. 312-322 ◽  
Author(s):  
Stefano Mangani ◽  
Manuela Benvenuti ◽  
Arthur J.G. Moir ◽  
Maria Ranieri-Raggi ◽  
Daniela Martini ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Amp Deaminase ◽  
Zinc Site

Structural Characterization of the Zinc Site in Protein Farnesyltransferase

2003 ◽  
Vol 125 (33) ◽  
pp. 9962-9969 ◽  
Author(s):  
Daniel A. Tobin ◽  
Jennifer S. Pickett ◽  
Heather L. Hartman ◽  
Carol A. Fierke ◽  
James E. Penner-Hahn
Keyword(s):  
Structural Characterization ◽  
Protein Farnesyltransferase ◽  
Zinc Site

scholarly journals Molecular dynamics study of zinc binding to cysteines in a peptide mimic of the alcohol dehydrogenase structural zinc site

2009 ◽  
Vol 11 (6) ◽  
pp. 975-983 ◽  
Author(s):  
Erik G. Brandt ◽  
Mikko Hellgren ◽  
Tore Brinck ◽  
Tomas Bergman ◽  
Olle Edholm
Keyword(s):  
Molecular Dynamics ◽  
Alcohol Dehydrogenase ◽  
Zinc Binding ◽  
Peptide Mimic ◽  
Zinc Site

Identification and tuning of zinc-site nitrogen-related complexes in ZnO material

2018 ◽  
Vol 36 (2) ◽  
pp. 021503
Author(s):  
Zhonghua Xu ◽  
Kun Tang ◽  
Shunming Zhu ◽  
Jingrui Ma ◽  
Jiandong Ye ◽  
...  
Keyword(s):  
Zinc Site

scholarly journals Allosteric histidine switch for regulation of intracellular zinc(II) fluctuation

2017 ◽  
Vol 114 (52) ◽  
pp. 13661-13666 ◽  
Author(s):  
Rongfeng Zhu ◽  
Yanqun Song ◽  
Haiping Liu ◽  
Yufei Yang ◽  
Shenlin Wang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Metal Binding ◽  
Transcriptional Activity ◽  
Transcriptional Regulator ◽  
Fine Tuning ◽  
Intracellular Zinc ◽  
Allosteric Control ◽  
Zinc Coordination ◽  
Dna Binding Affinity ◽  
Zinc Site

Metalloregulators allosterically control transcriptional activity through metal binding-induced reorganization of ligand residues and/or hydrogen bonding networks, while the coordination atoms on the same ligand residues remain seldom changed. Here we show that the MarR-type zinc transcriptional regulator ZitR switches one of its histidine nitrogen atoms for zinc coordination during the allosteric control of DNA binding. The Zn(II)-coordination nitrogen on histidine 42 within ZitR’s high-affinity zinc site (site 1) switches from Nε2 to Nδ1 upon Zn(II) binding to its low-affinity zinc site (site 2), which facilitates ZitR’s conversion from the nonoptimal to the optimal DNA-binding conformation. This histidine switch-mediated cooperation between site 1 and site 2 enables ZitR to adjust its DNA-binding affinity in response to a broad range of zinc fluctuation, which may allow the fine tuning of transcriptional regulation.

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