An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization

2015 ◽  
Vol 13 (17) ◽  
pp. 4859-4868 ◽  
Author(s):  
Rosa Vitale ◽  
Liliana Lista ◽  
Corinne Cerrone ◽  
Giorgio Caserta ◽  
Marco Chino ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Structural Characterization ◽  
Peroxidase Activity ◽  
Heme Protein ◽  
Functional Screening ◽  
Heme Enzyme ◽  
Protein Model ◽  
Rational Refinement

The rational refinement of function into the heme-protein model Mimochrome VI (MC6) resulted in a new analogue, FeIII-E2L(TD)-MC6, with an improved peroxidase activity.

Synthesis, structural characterization and catalytic activity of chlororuthenium(II) complexes with substituted Schiff base/phosphine ancillary ligands

2020 ◽  
Vol 75 (9-10) ◽  
pp. 851-857
Author(s):  
Chong Chen ◽  
Fule Wu ◽  
Jiao Ji ◽  
Ai-Quan Jia ◽  
Qian-Feng Zhang
Keyword(s):  
Schiff Base ◽  
Catalytic Activity ◽  
Structural Characterization ◽  
Room Temperature ◽  
Molecular Structures ◽  
Cationic Complex ◽  
Neutral Complex ◽  
Ancillary Ligands ◽  
X Ray ◽  
X Ray Crystallography

AbstractTreatment of [(η6-p-cymene)RuCl2]2 with one equivalent of chlorodiphenylphosphine in tetrahydrofuran at reflux afforded a neutral complex [(η6-p-cymene)RuCl2(κ1-P-PPh2OH)] (1). Similarly, the reaction of [Ru(bpy)2Cl2·2H2O] (bpy = 2,2′-bipyridine) and chlorodiphenylphosphine in methanol gave a cationic complex [Ru(bpy)2Cl(κ1-P-PPh2OCH3)](PF6) (2), while treatment of [RuCl2(PPh3)3] with [2-(C5H4N)CH=N(CH2)2N(CH3)2] (L1) in tetrahydrofuran at room temperature afforded a ruthenium(II) complex [Ru(PPh3)Cl2(κ3-N,N,N-L1)] (3). Interaction of the chloro-bridged complex [Ru(CO)2Cl2]n with one equivalent of [Ph2P(o-C6H4)CH=N(CH2)2N(CH3)2] (L2) led to the isolation of [Ru(CO)Cl2(κ3-P,N,N-L2)] (4). The molecular structures of the ruthenium(II) complexes 1–4 have been determined by single-crystal X-ray crystallography. The properties of the ruthenium(II) complex 4 as a hydrogenation catalyst for acetophenone were also tested.

Homolysis of the Eu−N Bond. Synthesis, Structural Characterization, and Catalytic Activity of Novel Europium(II) Complexes

2003 ◽  
Vol 22 (17) ◽  
pp. 3546-3552 ◽  
Author(s):  
Shaowu Wang ◽  
Shuangliu Zhou ◽  
Enhong Sheng ◽  
Meihua Xie ◽  
Kehua Zhang ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Structural Characterization ◽  
The Eu

Dual pathways of heme protein model compound reactions with carbon monoxide

1976 ◽  
Vol 98 (11) ◽  
pp. 3395-3396 ◽  
Author(s):  
John Cannon ◽  
Jon Geibel ◽  
Martha Whipple ◽  
T. G. Traylor
Keyword(s):  
Carbon Monoxide ◽  
Model Compound ◽  
Heme Protein ◽  
Protein Model

Preparation of porphyrin modified CO9S8 nanocomposites and application for colorimetric biosensing of H2O2

2018 ◽  
Vol 22 (09n10) ◽  
pp. 935-943 ◽  
Author(s):  
Yan Gao ◽  
Chunqiao Jin ◽  
Miaomiao Chen ◽  
Xixi Zhu ◽  
Min Fu ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Catalytic Activity ◽  
Peroxidase Activity ◽  
Catalytic Mechanism ◽  
Color Change ◽  
Colorimetric Detection ◽  
Buffer Solution ◽  
Hydrogen Peroxide Detection ◽  
Steady State Kinetics ◽  
One Step

Hydrogen peroxide detection has been widely applied in the fields of biology, medicine, and chemistry. Colorimetric detection of hydrogen peroxide has proven to be a fast and convenient method. In this work, 5,10,15,20-tetrakis(4-chlorophenyl) porphyrin modified Co[Formula: see text]S[Formula: see text] nanocomposites (H[Formula: see text]TClPP-Co[Formula: see text]S[Formula: see text] were prepared via a facile one-step hydrothermal method. H[Formula: see text]TClPP-Co[Formula: see text]S[Formula: see text] nanocomposites were demonstrated to possess an enhanced mimetic peroxidase activity toward the substrate, 3,3[Formula: see text],5,5[Formula: see text]-tetramethylbenzidine (TMB), which can be oxidized to oxTMB (oxidized TMB) in a buffer solution of hydrogen peroxide with a color change from colorless to blue. The catalytic activity of H[Formula: see text]TClPP-Co[Formula: see text]S[Formula: see text] was further analyzed by steady-state kinetics, and H[Formula: see text]TClPP-Co[Formula: see text]S[Formula: see text] had high affinity towards both TMB and H[Formula: see text]O[Formula: see text]. Furthermore, fluorescence and ESR data revealed that the catalytic mechanism of the peroxidase activity of H[Formula: see text]TClPP-Co[Formula: see text]S[Formula: see text] is due to hydroxyl radicals generated from decomposition of H[Formula: see text]O[Formula: see text]. Based on the catalytic activity of H[Formula: see text]TClPP-Co[Formula: see text]S[Formula: see text], a sensitive colorimetric sensor of H[Formula: see text]O[Formula: see text] with a detection limit of 6.803 [Formula: see text]M as well as a range of 7–100 [Formula: see text]M was designed.

Sign in / Sign up

Export Citation Format

Share Document