Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions

Abstract

Noncovalent weak interactions [hydrophobic interaction and hydrogen (H)-bond] play crucial roles in controlling the functions of biomolecules, and thus have been used to design artificial metalloproteins/metalloenzymes during the past few decades. In this review, we focus on the recent progresses in protein design by tuning the noncovalent interactions, including hydrophobic and H-bonding interactions. The topics include redesign and reuse of the heme pocket and other protein scaffolds, design of the heme protein interface, and de novo design of metalloproteins. The informations not only give insights into the metalloenzyme reaction mechanisms but also provide new reactions for future applications.

Green and efficient biosynthesis of indigo from indole by engineered myoglobins

“…A small heme protein, myoglobin (Mb), has been shown to be favourable for design of articial enzymes. [9][10][11][12][13][14][15][16][17][18][19][20][21][22] To develop a simple and economical approach to producing indigo from indole, Watanabe and co-workers constructed a H 2 O 2 -dependent catalytic oxidation system using Mb by replacement of the distal histidine (His64) with an aspartate, as well as other modications in the heme distal pocket. 23 Unfortunately, the best indigo yield obtained was only 12%, based on the consumed indole.…”

Rational design of heme enzymes for biodegradation of pollutants toward a green future

“…Meanwhile, their catalytic efficiencies were not high enough, which hindered general applications for bioremediation [14][15][16]. To overcome the limitations, rational design of artificial enzymes provides a chance to create more functional enzymes, such as for artificial oxidases and reductases [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32]. To date, impressive progress has also been made in the design of artificial enzymes for biodegradation [33][34][35][36][37][38][39].…”

Celebrating Helmut Sigel

“…Shun Hirota and his colleague review the recent progress in protein design, including redesign and reuse of the heme pocket and other protein scaffolds, design of the heme protein interface, as well as the de novo design of metalloproteins [19].…”