Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage

Biochemistry ◽  
1992 ◽  
Vol 31 (34) ◽  
pp. 7931-7938 ◽  
Author(s):  
Lynmarie K. Thompson ◽  
Ann E. McDermott ◽  
Jan Raap ◽  
C. M. Van der Wielen ◽  
Johan Lugtenburg ◽  
...  
Keyword(s):  
Schiff Base ◽  
Active Site ◽  
Site Structure ◽  
Rotational Resonance ◽  
Nmr Study ◽  
Active Site Structure

scholarly journals Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase fromNeisseriae meningitidis. A1H NMR Study

Biochemistry ◽  
2011 ◽  
Vol 50 (41) ◽  
pp. 8823-8833 ◽  
Author(s):  
Dungeng Peng ◽  
James D. Satterlee ◽  
Li-Hua Ma ◽  
Jerry L. Dallas ◽  
Kevin M. Smith ◽  
...  
Keyword(s):  
Heme Oxygenase ◽  
Active Site ◽  
Site Structure ◽  
Substrate Modification ◽  
Nmr Study ◽  
Active Site Structure ◽  
Influence Of Substrate

Solution 1H NMR study of the active site structure for the double mutant H64Q/V68F cyanide complex from mouse neuroglobin

2008 ◽  
Vol 136 (2-3) ◽  
pp. 115-123 ◽  
Author(s):  
Guowei Yin ◽  
Yanjie Li ◽  
Juan Li ◽  
Jing Li ◽  
Weihong Du ◽  
...  
Keyword(s):  
1H Nmr ◽  
Active Site ◽  
Double Mutant ◽  
Cyanide Complex ◽  
Site Structure ◽  
Nmr Study ◽  
Active Site Structure

scholarly journals Two-dimensional NMR Study of the Heme Active Site Structure of Chloroperoxidase

2002 ◽  
Vol 278 (10) ◽  
pp. 7765-7774 ◽  
Author(s):  
Xiaotang Wang ◽  
Hiroyasu Tachikawa ◽  
Xianwen Yi ◽  
Kelath M. Manoj ◽  
Lowell P. Hager
Keyword(s):  
Active Site ◽  
Two Dimensional ◽  
Site Structure ◽  
Nmr Study ◽  
Active Site Structure

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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