Expanding the applicability of cytochrome P450s and other haemoproteins

Ariyasu, Shinya; Stanfield, Joshua Kyle; Aiba, Yuichiro; Okada, Shoji

doi:10.1016/j.cbpa.2020.06.010

Cited by 34 publications

(29 citation statements)

References 63 publications

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“…P450 monooxygenases such as the enzyme from Bacillus megaterium (P450BM3) have been studied extensively for the ring-hydroxylation of benzene and its derivatives. [182][183][184][185][186][187] Especially in case of alkyl substituted arenes the regioselectivity can be rather poor, yielding complex mixtures of ring-and sidechain hydroxylated products. Enzyme engineering however can alleviate this issue.…”

Section: Aromatic Hydroxylation Reactionsmentioning

confidence: 99%

Biocatalysis making waves in organic chemistry

2022

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Section: Aromatic Hydroxylation Reactionsmentioning

confidence: 99%

Biocatalysis making waves in organic chemistry

2022

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“…TheM -CO distances for the other three CO ligands are rather similar (Supporting Information, Table S3). Mn ion and the ortho-O atom are confirmed metal-ligand cooperation sites.T heir distances in 1a and 1b are about 3.2 .N otably,t he distances of the Mn ion to the C6 or N2 atom in 1c and 1d,respectively,are only about 3.0 .T his short distance substantiates the possibility of the C6 and N2 atoms serving as an alternate metal-ligand cooperative site.U pon deprotonation of 1c to form 3(18crown-6), the C5-C6 bond shortened from 1.533(9) to 1.396(2) ,a nd the C5-O5 bond elongated from 1.216(7) to 1.250 (2) .T hese changes confirm the presence of acoordinating enolate moiety in 3(18-crown-6).…”

Section: Resultsmentioning

confidence: 82%

Diversifying Metal–Ligand Cooperative Catalysis in Semi‐Synthetic [Mn]‐Hydrogenases

et al. 2021

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The reconstitution of [Mn]-hydrogenases using as eries of Mn I complexes is described. These complexes are designed to have an internal base or pro-base that may participate in metal-ligand cooperative catalysis or have no internal base or pro-base.Only Mn I complexes with an internal base or pro-base are active for H 2 activation;o nly [Mn]hydrogenases incorporating such complexes are active for hydrogenase reactions.These results confirm the essential role of metal-ligand cooperation for H 2 activation by the Mn I complexes alone and by [Mn]-hydrogenases.O wing to the nature and position of the internal base or pro-base,the mode of metal-ligand cooperation in two active [Mn]-hydrogenases is different from that of the native [Fe]-hydrogenase.O ne [Mn]-hydrogenase has the highest specific activity of semisynthetic [Mn]-and [Fe]-hydrogenases.T his work demonstrates reconstitution of active artificial hydrogenases using synthetic complexes differing greatly from the native active site.

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“…As alternatives to natural enzymes, articial enzymes have received much attention for decades due to their potential applications, including in the environment. [14][15][16][17][18][19][20][21] With the advantages of high-yield of overexpression in E. coli cells, myoglobin (Mb), an O 2 carrier, has been favored for rational design of articial enzymes with multiple functions. 22 For example, Lu and colleagues rationally designed articial hemecopper oxidases and nitric oxide reductases by creating Cu B or Fe B metal-binding site in Mb.…”

Section: Introductionmentioning

confidence: 99%