Metal-Binding Affinity of the Transmembrane Site in ZntA:  Implications for Metal Selectivity†

Biochemistry ◽  
2006 ◽  
Vol 45 (3) ◽  
pp. 763-772 ◽  
Author(s):  
Junbo Liu ◽  
Sabari J. Dutta ◽  
Ann J. Stemmler ◽  
Bharati Mitra
Keyword(s):  
Binding Affinity ◽  
Metal Binding ◽  
Metal Selectivity

Structural and functional studies of SAV1707 from Staphylococcus aureus elucidate its distinct metal-dependent activity and a crucial residue for catalysis

2021 ◽  
Vol 77 (5) ◽  
pp. 587-598
Author(s):  
Dong-Gyun Kim ◽  
Kyu-Yeon Lee ◽  
Sang Jae Lee ◽  
Seung-Ho Cheon ◽  
Yuri Choi ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Metal Binding ◽  
Binding Mode ◽  
Structure And Function ◽  
Functional Study ◽  
Functional Studies ◽  
Dependent Endonuclease ◽  
Metal Selectivity ◽  
Metal Binding Domain ◽  
And Function

The metallo-β-lactamase fold is the most abundant metal-binding domain found in two major kingdoms: bacteria and archaea. Despite the rapid growth in genomic information, most of these enzymes, which may play critical roles in cellular metabolism, remain uncharacterized in terms of structure and function. In this study, X-ray crystal structures of SAV1707, a hypothetical metalloenzyme from Staphylococcus aureus, and its complex with cAMP are reported at high resolutions of 2.05 and 1.55 Å, respectively, with a detailed atomic description. Through a functional study, it was verified that SAV1707 has Ni2+-dependent phosphodiesterase activity and Mn2+-dependent endonuclease activity, revealing a different metal selectivity depending on the reaction. In addition, the crystal structure of cAMP-bound SAV1707 shows a unique snapshot of cAMP that reveals the binding mode of the intermediate, and a key residue Phe511 that forms π–π interactions with cAMP was verified as contributing to substrate recognition by functional studies of its mutant. Overall, these findings characterized the relationship between the structure and function of SAV1707 and may provide further understanding of metalloenzymes possessing the metallo-β-lactamase fold.

Metal-binding hydrazone photoswitches for visible light reactivity and variable relaxation kinetics

2017 ◽  
Vol 16 (11) ◽  
pp. 1604-1612 ◽  
Author(s):  
Kacey C. Hall ◽  
Andrew T. Franks ◽  
Rory C. McAtee ◽  
Michael S. Wang ◽  
Vivian I. Lu ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Visible Light ◽  
Binding Affinity ◽  
Blue Light ◽  
Metal Binding ◽  
Relaxation Kinetics ◽  
Photostationary State ◽  
State Composition

Photoactive aroylhydrazones demonstrate variability in UVA, UVC and blue light photoreactivity, photostationary state composition, photoisomer thermal stability, and relative iron(iii) binding affinity in ways that may inform metal-gated photoswitching applications.

scholarly journals Distinctive Trend of Metal Binding Affinity via Hydration Shell Breakage in Nanoconfined Cavity

2019 ◽  
Vol 123 (23) ◽  
pp. 14825-14833 ◽  
Author(s):  
Jiancheng Luo ◽  
Songtao Ye ◽  
Tao Li ◽  
Erik Sarnello ◽  
Hui Li ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Metal Binding ◽  
Hydration Shell

On-line coupling of continuous-flow gel electrophoresis with inductively coupled plasma-mass spectrometry to quantitatively evaluate intracellular metal binding properties of metallochaperones HpHypA and HpHspA in E. coli cells

Metallomics ◽  
2015 ◽  
Vol 7 (10) ◽  
pp. 1399-1406 ◽  
Author(s):  
Yuchuan Wang ◽  
Ligang Hu ◽  
Xinming Yang ◽  
Yuen-Yan Chang ◽  
Xuqiao Hu ◽  
...  
Keyword(s):  
Metal Binding ◽  
Inductively Coupled Plasma ◽  
Binding Properties ◽  
E Coli ◽  
Inductively Coupled ◽  
Metal Selectivity ◽  
Icp Ms ◽  
Plasma Mass Spectrometry ◽  
On Line ◽  
Line Coupling

Quantitative analysis of metal selectivity of overexpressed metalloproteins in cells by GE-ICP-MS.

Theoretical aspects of the enhancement of metal binding affinity by intramolecular hydrogen bonding and modulating pKavalues

2017 ◽  
Vol 41 (24) ◽  
pp. 15110-15119 ◽  
Author(s):  
Ahmad Motahari ◽  
Alireza Fattahi
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonding ◽  
Binding Affinity ◽  
Metal Binding ◽  
Intramolecular Hydrogen Bonding ◽  
Hydrogen Bond Network ◽  
Bond Network ◽  
The Stability ◽  
Intramolecular Hydrogen

The stability balance shows that the hydrogen bond network and modulation of pKavalues can enhance the metal binding affinity.

A histidine substitution confers metal binding affinity to a Schistosoma japonicum Glutathione S-transferase

2010 ◽  
Vol 73 (1) ◽  
pp. 74-77 ◽  
Author(s):  
Young-Hyun Han ◽  
Hee-Ah Seo ◽  
Ga-Hye Kim ◽  
Chung-Kyung Lee ◽  
Young Kee Kang ◽  
...  
Keyword(s):  
Schistosoma Japonicum ◽  
Binding Affinity ◽  
Metal Binding ◽  
Glutathione S Transferase
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