Resonance Raman study on the active-site structure of a cooperative hemerythrin

Biochemistry ◽  
1992 ◽  
Vol 31 (30) ◽  
pp. 6997-7002 ◽  
Author(s):  
Shoji Kaminaka ◽  
Hideo Takizawa ◽  
Takashi Handa ◽  
Hiroshi Kihara ◽  
Teizo Kitagawa
Keyword(s):  
Active Site ◽  
Resonance Raman ◽  
Site Structure ◽  
Raman Study ◽  
Active Site Structure

The Active Site Structure of Hemea33+C⋮NCuB2+of Cytochromeaa3Oxidase as Revealed from Resonance Raman Scattering

2003 ◽  
Vol 107 (36) ◽  
pp. 9865-9868 ◽  
Author(s):  
Eftychia Pinakoulaki ◽  
Magdalini Vamvouka ◽  
Constantinos Varotsis
Keyword(s):  
Raman Scattering ◽  
Active Site ◽  
Resonance Raman ◽  
Resonance Raman Scattering ◽  
Site Structure ◽  
Active Site Structure

Resonance raman spectra and the active site structure of semisynthetic Met80Cys horse heart cytochrome c

1994 ◽  
Vol 33 (21) ◽  
pp. 4629-4634 ◽  
Author(s):  
Giulietta Smulevich ◽  
Morten J. Bjerrum ◽  
Harry B. Gray ◽  
Thomas G. Spiro
Keyword(s):  
Cytochrome C ◽  
Raman Spectra ◽  
Active Site ◽  
Resonance Raman ◽  
Horse Heart Cytochrome ◽  
Site Structure ◽  
Active Site Structure ◽  
Resonance Raman Spectra ◽  
Horse Heart Cytochrome C

scholarly journals Active-site structure, binding and redox activity of the heme–thiolate enzyme CYP2D6 immobilized on coated Ag electrodes: a surface-enhanced resonance Raman scattering study

2007 ◽  
Vol 13 (1) ◽  
pp. 85-96 ◽  
Author(s):  
Alois Bonifacio ◽  
Diego Millo ◽  
Peter H. J. Keizers ◽  
Roald Boegschoten ◽  
Jan N. M. Commandeur ◽  
...  
Keyword(s):  
Raman Scattering ◽  
Active Site ◽  
Resonance Raman ◽  
Redox Activity ◽  
Resonance Raman Scattering ◽  
Site Structure ◽  
Ag Electrodes ◽  
Surface Enhanced ◽  
Scattering Study ◽  
Active Site Structure

The active site structure ofba3 oxidase fromThermus thermophilus studied by resonance Raman spectroscopy

1999 ◽  
Vol 5 (S5) ◽  
pp. S53-S63 ◽  
Author(s):  
S. Gerscher ◽  
P. Hildebrandt ◽  
G. Buse ◽  
T. Soulimane
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Site Structure ◽  
Active Site Structure

Distinct heme active-site structure in lactoperoxidase revealed by resonance Raman spectroscopy

Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 10125-10130 ◽  
Author(s):  
Songzhou Hu ◽  
Robert W. Treat ◽  
James R. Kincaid
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Site Structure ◽  
Active Site Structure

scholarly journals Differences in Active Site Structure in a Family of β-glucan Endohydrolases Deduced from the Kinetics of Inactivation by Epoxyalkyl β-Oligoglucosides

1989 ◽  
Vol 264 (9) ◽  
pp. 4939-4947
Author(s):  
P B Høj ◽  
E B Rodriguez ◽  
R V Stick ◽  
B A Stone
Keyword(s):  
Active Site ◽  
Site Structure ◽  
Active Site Structure ◽  
Kinetics Of

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

Effect of Histidine 6 Protonation on the Active Site Structure and Electron-Transfer Capabilities of Pseudoazurin fromAchromobacter cycloclastes†

Biochemistry ◽  
2002 ◽  
Vol 41 (1) ◽  
pp. 120-130 ◽  
Author(s):  
Katsuko Sato ◽  
Christopher Dennison
Keyword(s):  
Electron Transfer ◽  
Active Site ◽  
Site Structure ◽  
Active Site Structure

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.

The Effect of the Active-Site Structure on the Activity of Copper Mordenite in the Aerobic and Anaerobic Conversion of Methane into Methanol

2018 ◽  
Vol 57 (29) ◽  
pp. 8906-8910 ◽  
Author(s):  
Vitaly L. Sushkevich ◽  
Dennis Palagin ◽  
Jeroen A. van Bokhoven
Keyword(s):  
Active Site ◽  
Site Structure ◽  
Conversion Of Methane ◽  
Active Site Structure ◽  
Anaerobic Conversion ◽  
Aerobic And Anaerobic
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