Abstract:An artificial enzyme of F43H/H64 myoglobin was successfully applied for efficient biodegradation of malachite green, with the catalytic efficiency exceeding those of some natural enzymes.
“…The parameters of k cat and K m are listed in Table 1. The results showed that the k cat value of H64D Mb and F43H/H64D Mb are 0.1218 s −1 (87-fold vs. WT Mb 22 ) and 0.3148 s −1 (225-fold vs. WT Mb), respectively. These results indicate that the aspartic acid at the 64 position and the distal His43 could facilitate the catalytic ability, which agree with previous studies.…”
Section: Resultsmentioning
confidence: 96%
“…39 Moreover, heme enzymes such as lignin peroxidase, manganese peroxidase, and horseradish peroxidase were applied for the decolorization of MG. [18][19][20][21]41 Meanwhile, the catalytic efficiency of these native enzymes needs to be improved, and it is still required more efficient enzymes for biodegradation. For example, in a recent study, 22 we have realized MG degradation by an articial heme enzyme engineered in the protein scaffold of myoglobin (Mb), F43H/H64A Mb, with modication of the heme active site.…”
Engineered globins such as H64D Mb and A15C/H64D Ngb were efficient in the degradation of malachite green, with activities much higher than those of some native enzymes.
“…The parameters of k cat and K m are listed in Table 1. The results showed that the k cat value of H64D Mb and F43H/H64D Mb are 0.1218 s −1 (87-fold vs. WT Mb 22 ) and 0.3148 s −1 (225-fold vs. WT Mb), respectively. These results indicate that the aspartic acid at the 64 position and the distal His43 could facilitate the catalytic ability, which agree with previous studies.…”
Section: Resultsmentioning
confidence: 96%
“…39 Moreover, heme enzymes such as lignin peroxidase, manganese peroxidase, and horseradish peroxidase were applied for the decolorization of MG. [18][19][20][21]41 Meanwhile, the catalytic efficiency of these native enzymes needs to be improved, and it is still required more efficient enzymes for biodegradation. For example, in a recent study, 22 we have realized MG degradation by an articial heme enzyme engineered in the protein scaffold of myoglobin (Mb), F43H/H64A Mb, with modication of the heme active site.…”
Engineered globins such as H64D Mb and A15C/H64D Ngb were efficient in the degradation of malachite green, with activities much higher than those of some native enzymes.
“…More recent work employing a triple mutant based on the F43Y platform has achieved comparable catalytic efficiency to the most efficient native horseradish peroxidase (HRP), where the combination of T67R and F138W mutations is used to mimic the His-Arg pair and conserved Trp residues of native peroxidases . The scope of engineered Mb-based catalysts has also been expanded to biodegradation applications; for example, the F43H/H64A Mb mutant successfully catalyzed the biodegradation of malachite green (MG) with even higher efficiency than natural enzymes such as dye-decolorizing peroxidase and laccase . Molecular modeling indicates that these active site mutations favor the binding of MG in the heme distal pocket.…”
Section: Catalysis Beyond the Primary Coordination Sphere
By Heme Pro...mentioning
confidence: 99%
“…122 The scope of engineered Mb-based catalysts has also been expanded to biodegradation applications; for example, the F43H/H64A Mb mutant successfully catalyzed the biodegradation of malachite green (MG) with even higher efficiency than natural enzymes such as dye-decolorizing peroxidase and laccase. 123 Molecular modeling indicates that these active site mutations favor the binding of MG in the heme distal pocket.…”
Section: Rational Design Using Myoglobin As a Scaffoldmentioning
Metalloenzymes catalyze a variety of reactions using
a limited
number of natural amino acids and metallocofactors. Therefore, the
environment beyond the primary coordination sphere must play an important
role in both conferring and tuning their phenomenal catalytic properties,
enabling active sites with otherwise similar primary coordination
environments to perform a diverse array of biological functions. However,
since the interactions beyond the primary coordination sphere are
numerous and weak, it has been difficult to pinpoint structural features
responsible for the tuning of activities of native enzymes. Designing
artificial metalloenzymes (ArMs) offers an excellent basis to elucidate
the roles of these interactions and to further develop practical biological
catalysts. In this review, we highlight how the secondary coordination
spheres of ArMs influence metal binding and catalysis, with particular
focus on the use of native protein scaffolds as templates for the
design of ArMs by either rational design aided by computational modeling,
directed evolution, or a combination of both approaches. In describing
successes in designing heme, nonheme Fe, and Cu metalloenzymes, heteronuclear
metalloenzymes containing heme, and those ArMs containing other metal
centers (including those with non-native metal ions and metallocofactors),
we have summarized insights gained on how careful controls of the
interactions in the secondary coordination sphere, including hydrophobic
and hydrogen bonding interactions, allow the generation and tuning
of these respective systems to approach, rival, and, in a few cases,
exceed those of native enzymes. We have also provided an outlook on
the remaining challenges in the field and future directions that will
allow for a deeper understanding of the secondary coordination sphere
a deeper understanding of the secondary coordintion sphere to be gained,
and in turn to guide the design of a broader and more efficient variety
of ArMs.
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