Metal and metal-oxide nanozymes: bioenzymatic characteristics, catalytic mechanism, and eco-environmental applications

Nanoscale ◽  
2019 ◽  
Vol 11 (34) ◽  
pp. 15783-15793 ◽  
Author(s):  
Wenjun Chen ◽  
Shunyao Li ◽  
Jun Wang ◽  
Kai Sun ◽  
Youbin Si

This review highlights the available studies on the enzymatic characteristics and catalytic mechanisms of natural enzymes and artificial metal and metal-oxide nanozymes in the removal and transformation of phenolic contaminants.

2005 ◽  
Vol 83 (4) ◽  
pp. 497-504 ◽  
Author(s):  
Benoit Coulombe ◽  
Marie-France Langelier

High resolution X-ray crystal structures of multisubunit RNA polymerases (RNAP) have contributed to our understanding of transcriptional mechanisms. They also provided a powerful guide for the design of experiments aimed at further characterizing the molecular stages of the transcription reaction. Our laboratory used tandem-affinity peptide purification in native conditions to isolate human RNAP II variants that had site-specific mutations in structural elements located strategically within the enzyme's catalytic center. Both in vitro and in vivo analyses of these mutants revealed novel features of the catalytic mechanisms involving this enzyme.Key words: RNA polymerase II, transcriptional mechanisms, mutational analysis, mRNA synthesis.


2020 ◽  
Author(s):  
zheng zhao ◽  
Phil bourne ◽  
Hao Hu ◽  
Huanyu Chu

Acylphosphatase is one of the vital enzymes in many organs/tissues to catalyze an acylphosphate molecule into carboxylate and phosphate. Here we use a combined <i>ab initio</i> QM/MM approach to reveal the catalytic mechanism of the benzoylphosphate-bound acylphosphatase system. Using a multi-dimensional reaction-coordinates-driving scheme, we obtained a detailed catalytic process including one nucleophilic-attack and then an ensuing carbonyl-shuttle catalytic mechanism by calculating two-dimensional potential energy surfaces. We also obtained an experiment-agreeable energy barrier and validated the role of the key amino acid Asn38. Additionally, we qualified the transition state stabilization strategy based on the amino acids-contributed interaction networks revealed in the enzymatic environment. This study provided usefule insights into the underlying catalytic mechanism to contribute to disease-involved research.


2015 ◽  
Vol 13 (41) ◽  
pp. 10262-10272 ◽  
Author(s):  
Debasish Bhowmick ◽  
Govindasamy Mugesh

This review focuses on the variation of the catalytic mechanisms of synthetic glutathione peroxidase (GPx) mimics depending on their structures and reactivities towards thiols and peroxides. Compounds of different categories follow a characteristic mechanism for the reduction of peroxides.


2021 ◽  
Vol 9 ◽  
Author(s):  
Peng Wang ◽  
Dongyu Min ◽  
Guoyou Chen ◽  
Minghui Li ◽  
Liquan Tong ◽  
...  

In recent years, with the development of nanomaterials, a slice of nanomaterials has been demonstrated to possess high catalytic activity similar to natural enzymes and counter the dilemmas including easy inactivation and low yield natural of enzymes, which are labeled as nanozymes. The catalytic activity of nanozymes could be easily regulated by size, structure, surface modification and other factors. In comparison with natural enzymes, nanozymes featured with a more stable structure, economical preparation and preservation, diversity of functions and adjustable catalytic activity, thus becoming the potentially ideal substitute for natural enzymes. Generally, the are mainly three types containing metal oxide nanozymes, noble metal nanozymes and carbon-based nanozymes, owing various applications in biomedical, energy and environmental fields. In this review, to summarize the recent representative applications of nanozymes, and potentially explore the scientific problems in this field at the same time, we are going to discuss the catalytic mechanisms of diverse nanozymes, with the emphasis on their applications in the fields of tumor therapy, anti-inflammatory and biosensing, hoping to help and guide the future development of nanozymes.


Author(s):  
Ming Du ◽  
Lu Zhang

Hydrogenase plays an important role in the process of biohydrogen production. Hydrogenases have very unique active sites and are classified into three groups according to the metal composition of the active sites: the [Ni-Fe] hydrogenase, [Fe-Fe] hydrogenase, and [Fe-only] hydrogenase. In this paper, the crystal structures and active sites of three kinds of hydrogenases are examined and compared. These enzymes have an unusual structural feature in common. Their similar active site indicates that the catalytic mechanism of hydrogen activation is probably similar. The understanding of the catalytic mechanisms for the three kinds of hydrogenases may help achieve the industrialization process of hydrogen energy production. Moreover, the future research direction about the hydrogenases from auto-aggregative bacteria and the chemical mimic of hydrogenases structure is discussed.


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