14 publications

14 publications

Catalytic Cyclopropanation by Myoglobin Reconstituted with Iron Porphycene: Acceleration of Catalysis due to Rapid Formation of the Carbene Species

Hasegawa, J.-Y.; Lehnert, N.

J. Am. Chem. Soc., 2017, 10.1021/jacs.7b10154


Metal: Fe
Ligand type: Amino acid; Porphycene
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: ---
Reaction: Cyclopropanation
Max TON: ---
ee: ---
PDB: ---
Notes: Cyclopropanation of styrene with ethyl diazoacetate: kcat/KM = 1.3 mM-1 * s-1, trans/cis = 99:1

Coordinated Design of Cofactor and Active Site Structures in Development of New Protein Catalysts

Watanabe, Y.

J. Am. Chem. Soc., 2005, 10.1021/ja045995q


Metal: Mn
Ligand type: Salophen
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: 1V9Q
Notes: ---

Metal: Cr
Ligand type: Salophen
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: 1J3F
Notes: ---

Metal: Mn
Ligand type: Salen
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Metal: Cr
Ligand type: Salen
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Crystal Structure and Peroxidase Activity of Myoglobin Reconstituted with Iron Porphycene

Inorg. Chem., 2006, 10.1021/ic061130x


Metal: Fe
Ligand type: Porphycene
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: ---
Max TON: ---
ee: ---
PDB: 1MBI
Notes: ---

C(sp3)–H Bond Hydroxylation Catalyzed by Myoglobin Reconstituted with Manganese Porphycene

Hayashi, T

J. Am. Chem. Soc., 2013, 10.1021/ja409404k


Metal: Mn
Ligand type: Porphycene
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: ---
Reaction: Hydroxylation
Max TON: ---
ee: ---
PDB: 2WI8
Notes: ---

Design of Metal Cofactors Activated by a Protein–Protein Electron Transfer System

Ueno, T.

Proc. Natl. Acad. Sci. U. S. A., 2006, 10.1073/pnas.0510968103


Metal: Fe
Ligand type: Salophen
Host protein: Heme oxygenase (HO)
Anchoring strategy: Reconstitution
Optimization: Chemical
Reaction: O2 reduction
Max TON: ---
ee: ---
PDB: 1WZD
Notes: ---

Generation of a Functional, Semisynthetic [FeFe]-Hydrogenase in a Photosynthetic Microorganism

Berggren, G.; Lindblad, P.

Energy Environ. Sci., 2018, 10.1039/C8EE01975D


Metal: Fe
Ligand type: CN; CO
Anchoring strategy: Reconstitution
Optimization: Chemical & genetic
Reaction: H2 evolution
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Hybridization of Modified-Heme Reconstitution and Distal Histidine Mutation to Functionalize Sperm Whale Myoglobin

J. Am. Chem. Soc., 2004, 10.1021/ja038798k


Metal: Fe
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: Genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Manganese(V) Porphycene Complex Responsible for Inert C–H Bond Hydroxylation in a Myoglobin Matrix

Oohora, K.

J. Am. Chem. Soc., 2017, 10.1021/jacs.7b11288


Metal: Mn
Ligand type: Amino acid; Porphycene
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: ---
Reaction: Hydroxylation
Max TON: 13
ee: ---
PDB: 5YL3
Notes: ---

Meso-Unsubstituted Iron Corrole in Hemoproteins: Remarkable Differences in Effects on Peroxidase Activities between Myoglobin and Horseradish Peroxidase

J. Am. Chem. Soc., 2009, 10.1021/ja907428e


Metal: Fe
Ligand type: Corrole
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Metal: Fe
Ligand type: Corrole
Anchoring strategy: Reconstitution
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Orthogonal Expression of an Artificial Metalloenzyme for Abiotic Catalysis

Brustad, E. M.

ChemBioChem, 2017, 10.1002/cbic.201700397


Metal: Ir
Ligand type: Methyl; Porphyrin
Host protein: Cytochrome BM3h
Anchoring strategy: Reconstitution
Optimization: Chemical & genetic
Reaction: Cyclopropanation
Max TON: 339
ee: 97
PDB: ---
Notes: Reaction of styrene with ethyl diazoacetate, cis:trans = 29:71

Peroxidase Activity of Myoglobin is Enhanced by Chemical Mutation of Heme-Propionates

J. Am. Chem. Soc., 1999, 10.1021/ja9841005


Metal: Fe
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Porphyrinoid Chemistry in Hemoprotein Matrix:  Detection and Reactivities of Iron(IV)-Oxo Species of Porphycene Incorporated into Horseradish Peroxidase

J. Am. Chem. Soc., 2007, 10.1021/ja074685f


Metal: Fe
Ligand type: Porphycene
Anchoring strategy: Reconstitution
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Precise Design of Artificial Cofactors for Enhancing Peroxidase Activity of Myoglobin: Myoglobin Mutant H64D Reconstituted with a “Single-Winged Cofactor” is Equivalent to Native Horseradish Peroxidase in Oxidation Activity

Matsuo, T.

Chem. - Asian J., 2011, 10.1002/asia.201100107


Metal: Fe
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Preparation of Artificial Metalloenzymes by Insertion of Chromium(III) Schiff Base Complexes into apo-Myoglobin Mutants

Watanabe, Y.

Angew. Chem., Int. Ed., 2003, 10.1002/anie.200390256


Metal: Cr
Ligand type: Salophen
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: Genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---