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Catalytic mechanism in artificial metalloenzyme: QM/MM study of phenylacetylene polymerization by rhodium complex encapsulated in apo-Ferritin.

Artificial metalloenzyme, composed of metal complex(es) and a host protein, is a promising way to mimic enzyme catalytic functions or develop novel enzyme-like catalysis. However, it is highly challenging to unveil the active site and exact reaction mechanism inside artificial metalloenzyme, which i... Full description

Journal Title: Journal of the American Chemical Society September 19, 2012, Vol.134(37), pp.15418-15429
Main Author: Ke, Zhuofeng
Other Authors: Abe, Satoshi , Ueno, Takafumi , Morokuma, Keiji
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; DOI: 1520-5126
Link: http://search.proquest.com/docview/1041325357/?pq-origsite=primo
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title: Catalytic mechanism in artificial metalloenzyme: QM/MM study of phenylacetylene polymerization by rhodium complex encapsulated in apo-Ferritin.
format: Article
creator:
  • Ke, Zhuofeng
  • Abe, Satoshi
  • Ueno, Takafumi
  • Morokuma, Keiji
subjects:
  • Acetylene–Analogs & Derivatives
  • Catalysis–Chemistry
  • Crystallography, X-Ray–Metabolism
  • Enzymes–Chemistry
  • Ferritins–Chemistry
  • Models, Molecular–Chemistry
  • Polymers–Chemistry
  • Quantum Theory–Chemistry
  • Rhodium–Chemistry
  • Enzymes
  • Polymers
  • Phenylacetylene
  • Ferritins
  • Rhodium
  • Acetylene
ispartof: Journal of the American Chemical Society, September 19, 2012, Vol.134(37), pp.15418-15429
description: Artificial metalloenzyme, composed of metal complex(es) and a host protein, is a promising way to mimic enzyme catalytic functions or develop novel enzyme-like catalysis. However, it is highly challenging to unveil the active site and exact reaction mechanism inside artificial metalloenzyme, which is the bottleneck in its rational design. We present a QM/MM study of the complicated reaction mechanism for the recently developed artificial metalloenzyme system, (Rh(nbd)·apo-Fr) (nbd = norbornadiene), which is composed of a rhodium complex [Rh(nbd)Cl](2) and the recombinant horse L-chain apo-Ferritin. We found that binding sites suggested by the X-ray crystal structure, i.e., sites A, B, and C, are only precursors/intermediates, not true active sites for polymerization of phenylacetylene (PA). A new hydrophobic site, which we name D, is suggested to be the most plausible active site for polymerization. Active site D is generated after coordination of first monomer PA by extrusion of the Rh(I)(PA) complex to a hydrophobic pocket near site B. Polymerization occurs in site D via a Rh(I)-insertion mechanism. A specific "hydrophobic region" composed by the hydrophobic active site D, the nonpolar 4-fold channel, and other hydrophobic residues nearby is found to facilitate accumulation, coordination, and insertion of PA for polymerization. Our results also demonstrate that the hydrophobic active site D can retain the native regio- and stereoselectivity of the Rh-catalyzed polymerization of PA without protein. This study highlights the importance of theoretical study in mechanistic elucidation and rational design of artificial metalloenzymes, indicating that even with X-ray crystal structures at hand we may still be far from fully understanding the active site and catalytic mechanism of artificial metalloenzymes.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; DOI: 1520-5126
fulltext: no_fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


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titleCatalytic mechanism in artificial metalloenzyme: QM/MM study of phenylacetylene polymerization by rhodium complex encapsulated in apo-Ferritin.
creatorKe, Zhuofeng ; Abe, Satoshi ; Ueno, Takafumi ; Morokuma, Keiji
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identifierE-ISSN: 1520-5126 ; DOI: 1520-5126
subjectAcetylene–Analogs & Derivatives ; Catalysis–Chemistry ; Crystallography, X-Ray–Metabolism ; Enzymes–Chemistry ; Ferritins–Chemistry ; Models, Molecular–Chemistry ; Polymers–Chemistry ; Quantum Theory–Chemistry ; Rhodium–Chemistry ; Enzymes ; Polymers ; Phenylacetylene ; Ferritins ; Rhodium ; Acetylene
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descriptionArtificial metalloenzyme, composed of metal complex(es) and a host protein, is a promising way to mimic enzyme catalytic functions or develop novel enzyme-like catalysis. However, it is highly challenging to unveil the active site and exact reaction mechanism inside artificial metalloenzyme, which is the bottleneck in its rational design. We present a QM/MM study of the complicated reaction mechanism for the recently developed artificial metalloenzyme system, (Rh(nbd)·apo-Fr) (nbd = norbornadiene), which is composed of a rhodium complex [Rh(nbd)Cl](2) and the recombinant horse L-chain apo-Ferritin. We found that binding sites suggested by the X-ray crystal structure, i.e., sites A, B, and C, are only precursors/intermediates, not true active sites for polymerization of phenylacetylene (PA). A new hydrophobic site, which we name D, is suggested to be the most plausible active site for polymerization. Active site D is generated after coordination of first monomer PA by extrusion of the Rh(I)(PA) complex to a hydrophobic pocket near site B. Polymerization occurs in site D via a Rh(I)-insertion mechanism. A specific "hydrophobic region" composed by the hydrophobic active site D, the nonpolar 4-fold channel, and other hydrophobic residues nearby is found to facilitate accumulation, coordination, and insertion of PA for polymerization. Our results also demonstrate that the hydrophobic active site D can retain the native regio- and stereoselectivity of the Rh-catalyzed polymerization of PA without protein. This study highlights the importance of theoretical study in mechanistic elucidation and rational design of artificial metalloenzymes, indicating that even with X-ray crystal structures at hand we may still be far from fully understanding the active site and catalytic mechanism of artificial metalloenzymes.
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