Enzymes are complex biomacromolecules that are known to catalyze more than 5000 biological processes involving oxidation-reduction, group transfer, hydrolysis, isomerization and ligation. They provide tremendous rate acceleration (1010 – 1015-fold) and extremely high selectivity. Over one-third of natural enzymes contain metal ions, mostly one or two, at their active sites. These ions play critical roles in the functioning of metalloenzymes by providing structural and catalytic functions. The enzyme-catalyzed reactions have been implicated in a wide range of biological, biotechnological, pharmaceutical and industrial applications. Despite the availability of numerous natural enzymes, currently only a few of them have been used for such applications, frequently with some shortcomings. A majority of enzymes function under narrow temperature and pH conditions, exhibit broad specificities, and are expensive. Thus, the development of efficient, environmentally friendly, and economical synthetic analogues of metalloenzymes--also called artificial metalloenzymes--is highly desirable. They include multiple classes of these analogues such as metal complexes, supramolecular, polymeric, nanoparticulate, small organometallic complexes, and metal organic frameworks. These protein mimics can offer the following advantages over natural enzymes: (1) they are inexpensive and may be recyclable, (2) being smaller in size they impose little or no steric constraints, and (3) they can be tuned for specific applications. Additionally, they can provide a powerful platform for elucidating mechanisms of natural systems.
The rational design of efficient artificial metalloenzymes is a formidable task that necessitates a great deal of interdisciplinary cooperation. It is generally performed either through physico-chemical intuition of protein structure or using computational methods. In the last few decades, remarkable progress has been made in this area to mimic both structural and functional aspects of natural metalloenzymes. It has led to the development of the aforementioned classes of their synthetic analogues. However, it is not surprising that in comparison to natural enzymes, the reactions promoted by almost all of their synthetic counterparts are substantially slower, exhibit low selectivity, and occur with lower catalytic turnover. Thus, the rational design of artificial metalloenzymes continues to be a very intensive area of research.
The present Research Topic welcomes original articles and reviews regarding all aspects of artificial metalloenzyme research, including design, characterization, structure, and mechanism.
Enzymes are complex biomacromolecules that are known to catalyze more than 5000 biological processes involving oxidation-reduction, group transfer, hydrolysis, isomerization and ligation. They provide tremendous rate acceleration (1010 – 1015-fold) and extremely high selectivity. Over one-third of natural enzymes contain metal ions, mostly one or two, at their active sites. These ions play critical roles in the functioning of metalloenzymes by providing structural and catalytic functions. The enzyme-catalyzed reactions have been implicated in a wide range of biological, biotechnological, pharmaceutical and industrial applications. Despite the availability of numerous natural enzymes, currently only a few of them have been used for such applications, frequently with some shortcomings. A majority of enzymes function under narrow temperature and pH conditions, exhibit broad specificities, and are expensive. Thus, the development of efficient, environmentally friendly, and economical synthetic analogues of metalloenzymes--also called artificial metalloenzymes--is highly desirable. They include multiple classes of these analogues such as metal complexes, supramolecular, polymeric, nanoparticulate, small organometallic complexes, and metal organic frameworks. These protein mimics can offer the following advantages over natural enzymes: (1) they are inexpensive and may be recyclable, (2) being smaller in size they impose little or no steric constraints, and (3) they can be tuned for specific applications. Additionally, they can provide a powerful platform for elucidating mechanisms of natural systems.
The rational design of efficient artificial metalloenzymes is a formidable task that necessitates a great deal of interdisciplinary cooperation. It is generally performed either through physico-chemical intuition of protein structure or using computational methods. In the last few decades, remarkable progress has been made in this area to mimic both structural and functional aspects of natural metalloenzymes. It has led to the development of the aforementioned classes of their synthetic analogues. However, it is not surprising that in comparison to natural enzymes, the reactions promoted by almost all of their synthetic counterparts are substantially slower, exhibit low selectivity, and occur with lower catalytic turnover. Thus, the rational design of artificial metalloenzymes continues to be a very intensive area of research.
The present Research Topic welcomes original articles and reviews regarding all aspects of artificial metalloenzyme research, including design, characterization, structure, and mechanism.
