Complimenting a Metal Complex with Protein Environment toward a New Hybrid Biocatalyst
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- Hayashi Takashi
- Graduate School of Engineering, Osaka Univeristy
Bibliographic Information
- Other Title
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- 金属錯体とタンパク質反応場の融合:新規生体触媒へのアプローチ
- キンゾク サクタイ ト タンパクシツ ハンノウジョウ ノ ユウゴウ : シンキ セイタイ ショクバイ エ ノ アプローチ
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Abstract
Efforts to develop an attractive biocatalyst with new chemical reactivity and selectivity indicate that promising strategies involve the construction of artificial metalloenzymes generated by incorporation of a metal-containing moiety into a protein scaffold. In this article, we present three recent results focusing on the modification of proteins with artificial metal complexes. First, an artificial hydrogenase model containing a synthetic diiron carbonyl cluster, (µ-S2)[FeI(CO)3]2, held by a native cysteine-containing motif in the cytochrome c protein is described. The diiron carbonyl core anchored by coordination within the protein matrix works well as a catalyst for H2 evolution. Second, a hybrid catalyst containing a rhodium complex with a maleimide moiety at the peripheral position of the cyclopendiene ligand is described. The rhodium complex was inserted into a β-barrel protein scaffold of a mutant of aponitrobindin via a covalent linkage. The hybrid protein acts as a polymerization catalyst and preferentially yields trans-poly(phenylacetylene)(PPA). Finally, an artificial hemoprotein containing an iron porphycene, a structural isomer of hemin, within a heme pocket, is reported. The reconstituted horseradish peroxidase catalyzes the H2O2-dependent oxidation of thioanisole, of which the initial rate is 12-fold faster than that observed for native myoglobin.
Journal
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- Journal of Synthetic Organic Chemistry, Japan
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Journal of Synthetic Organic Chemistry, Japan 71 (5), 452-460, 2013
The Society of Synthetic Organic Chemistry, Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390282680318311424
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- NII Article ID
- 10031171536
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- NII Book ID
- AN0024521X
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- COI
- 1:CAS:528:DC%2BC3sXosVOrtrs%3D
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- ISSN
- 18836526
- 00379980
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- NDL BIB ID
- 024663806
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed