Active Site Structure of Photoactive Yellow Protein with a Locked Chromophore Analogue Revealed by Near-Infrared Raman Optical Activity

2013 ◽  
Vol 4 (18) ◽  
pp. 3031-3038 ◽  
Author(s):  
Kensuke Kubota ◽  
Takahito Shingae ◽  
Nicole D. Foster ◽  
Masato Kumauchi ◽  
Wouter D. Hoff ◽  
...  
Keyword(s):  
Optical Activity ◽  
Active Site ◽  
Near Infrared ◽  
Photoactive Yellow Protein ◽  
Site Structure ◽  
Raman Optical Activity ◽  
Active Site Structure

Exploring the Active Site Structure of Photoreceptor Proteins by Raman Optical Activity

2010 ◽  
Author(s):  
Masashi Unno ◽  
Takahito Shingae ◽  
Takashi Kikukawa ◽  
Naoki Kamo ◽  
P. M. Champion ◽  
...  
Keyword(s):  
Optical Activity ◽  
Active Site ◽  
Site Structure ◽  
Raman Optical Activity ◽  
Active Site Structure

Exploring the Active Site Structure of a Photoreceptor Protein by Raman Optical Activity

2013 ◽  
Vol 117 (5) ◽  
pp. 1321-1325 ◽  
Author(s):  
Masashi Unno ◽  
Takashi Kikukawa ◽  
Masato Kumauchi ◽  
Naoki Kamo
Keyword(s):  
Optical Activity ◽  
Active Site ◽  
Site Structure ◽  
Raman Optical Activity ◽  
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

Raman Optical Activity Probing Structural Deformations of the 4-Hydroxycinnamyl Chromophore in Photoactive Yellow Protein

2013 ◽  
Vol 4 (8) ◽  
pp. 1322-1327 ◽  
Author(s):  
Takahito Shingae ◽  
Kensuke Kubota ◽  
Masato Kumauchi ◽  
Fumio Tokunaga ◽  
Masashi Unno
Keyword(s):  
Optical Activity ◽  
Photoactive Yellow Protein ◽  
Raman Optical Activity ◽  
Structural Deformations

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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