Synthetic model approach to the active site structure of cytochrome oxidase. Novel porphyrin-containing heterobinuclear iron(III)-copper(II) complexes

1981 ◽  
Vol 103 (22) ◽  
pp. 6784-6787 ◽  
Author(s):  
Maxwell J. Gunter ◽  
Lewis N. Mander ◽  
Keith S. Murray ◽  
Paul E. Clark
Keyword(s):  
Cytochrome Oxidase ◽  
Active Site ◽  
Site Structure ◽  
Synthetic Model ◽  
Active Site Structure ◽  
Model Approach

Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo

1993 ◽  
Vol 25 (2) ◽  
pp. 121-136 ◽  
Author(s):  
Jonathan P. Hosler ◽  
Shelagh Ferguson-Miller ◽  
Melissa W. Calhoun ◽  
Jeffrey W. Thomas ◽  
John Hill ◽  
...  
Keyword(s):  
Cytochrome Oxidase ◽  
Active Site ◽  
Structure And Function ◽  
Site Structure ◽  
Active Site Structure ◽  
And Function ◽  
Insight Into

Active site structure and catalytic mechanisms of human peroxidases

2006 ◽  
Vol 445 (2) ◽  
pp. 199-213 ◽  
Author(s):  
Paul G. Furtmüller ◽  
Martina Zederbauer ◽  
Walter Jantschko ◽  
Jutta Helm ◽  
Martin Bogner ◽  
...  
Keyword(s):  
Active Site ◽  
Site Structure ◽  
Active Site Structure ◽  
Catalytic Mechanisms

scholarly journals Iron-Imprinted Single-Atomic Site Catalyst-Based Nanoprobe for Detection of Hydrogen Peroxide in Living Cells

2021 ◽  
Vol 13 (1) ◽  
Author(s):  
Zhaoyuan Lyu ◽  
Shichao Ding ◽  
Maoyu Wang ◽  
Xiaoqing Pan ◽  
Zhenxing Feng ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Active Site ◽  
Single Atom ◽  
Site Structure ◽  
Atomic Site ◽  
Ion Imprinting ◽  
Active Site Structure ◽  
In Situ Detection ◽  
Colorimetric Biosensing

AbstractFe-based single-atomic site catalysts (SASCs), with the natural metalloproteases-like active site structure, have attracted widespread attention in biocatalysis and biosensing. Precisely, controlling the isolated single-atom Fe-N-C active site structure is crucial to improve the SASCs’ performance. In this work, we use a facile ion-imprinting method (IIM) to synthesize isolated Fe-N-C single-atomic site catalysts (IIM-Fe-SASC). With this method, the ion-imprinting process can precisely control ion at the atomic level and form numerous well-defined single-atomic Fe-N-C sites. The IIM-Fe-SASC shows better peroxidase-like activities than that of non-imprinted references. Due to its excellent properties, IIM-Fe-SASC is an ideal nanoprobe used in the colorimetric biosensing of hydrogen peroxide (H2O2). Using IIM-Fe-SASC as the nanoprobe, in situ detection of H2O2 generated from MDA-MB-231 cells has been successfully demonstrated with satisfactory sensitivity and specificity. This work opens a novel and easy route in designing advanced SASC and provides a sensitive tool for intracellular H2O2 detection.

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