BesC Initiates C–C Cleavage through a Substrate-Triggered and Reactive Diferric-Peroxo Intermediate

2021 ◽  
Author(s):  
Olivia M. Manley ◽  
Haoyu Tang ◽  
Shan Xue ◽  
Yisong Guo ◽  
Wei-chen Chang ◽  
...  
Keyword(s):  
Peroxo Intermediate

Formation of an End-On Ferric Peroxo Intermediate upon One-Electron Reduction of a Ferric Superoxo Heme

2010 ◽  
Vol 132 (11) ◽  
pp. 3672-3673 ◽  
Author(s):  
Jin-Gang Liu ◽  
Yuta Shimizu ◽  
Takehiro Ohta ◽  
Yoshinori Naruta
Keyword(s):  
Electron Reduction ◽  
Ferric Peroxo ◽  
Peroxo Intermediate

scholarly journals Isolation of a Ru(iv) side-on peroxo intermediate in the water oxidation reaction

2021 ◽  
Author(s):  
Carla Casadevall ◽  
Vlad Martin-Diaconescu ◽  
Wesley R. Browne ◽  
Sergio Fernández ◽  
Federico Franco ◽  
...  
Keyword(s):  
Water Oxidation ◽  
Oxidation Reaction ◽  
Peroxo Intermediate

Mössbauer Studies of the Formation and Reactivity of a Quasi-Stable Peroxo Intermediate of Stearoyl-Acyl Carrier Protein Δ9-Desaturase†

Biochemistry ◽  
1999 ◽  
Vol 38 (38) ◽  
pp. 12197-12204 ◽  
Author(s):  
John A. Broadwater ◽  
Catalina Achim ◽  
Eckard Münck ◽  
Brian G. Fox
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Mössbauer Studies ◽  
Δ9 Desaturase ◽  
Peroxo Intermediate

A Ferric–Peroxo Intermediate in the Oxidation of Heme by IsdI

Biochemistry ◽  
2015 ◽  
Vol 54 (16) ◽  
pp. 2613-2621 ◽  
Author(s):  
Shin-ichi J. Takayama ◽  
Slade A. Loutet ◽  
A. Grant Mauk ◽  
Michael E. P. Murphy
Keyword(s):  
Ferric Peroxo ◽  
Peroxo Intermediate

scholarly journals Crystal structures of alkylperoxo and anhydride intermediates in an intradiol ring-cleaving dioxygenase

2014 ◽  
Vol 112 (2) ◽  
pp. 388-393 ◽  
Author(s):  
Cory J. Knoot ◽  
Vincent M. Purpero ◽  
John D. Lipscomb
Keyword(s):  
Ring Cleavage ◽  
Site Specificity ◽  
Computational Studies ◽  
Structural Comparison ◽  
Alternative Substrate ◽  
Extradiol Dioxygenase ◽  
X Ray ◽  
Solution Studies ◽  
Extradiol Dioxygenases ◽  
Peroxo Intermediate

Intradiol aromatic ring-cleaving dioxygenases use an active site, nonheme Fe3+ to activate O2 and catecholic substrates for reaction. The inability of Fe3+ to directly bind O2 presents a mechanistic conundrum. The reaction mechanism of protocatechuate 3,4-dioxygenase is investigated here using the alternative substrate 4-fluorocatechol. This substrate is found to slow the reaction at several steps throughout the mechanistic cycle, allowing the intermediates to be detected in solution studies. When the reaction was initiated in an enzyme crystal, it was found to halt at one of two intermediates depending on the pH of the surrounding solution. The X-ray crystal structure of the intermediate at pH 6.5 revealed the key alkylperoxo-Fe3+ species, and the anhydride-Fe3+ intermediate was found for a crystal reacted at pH 8.5. Intermediates of these types have not been structurally characterized for intradiol dioxygenases, and they validate four decades of spectroscopic, kinetic, and computational studies. In contrast to our similar in crystallo crystallographic studies of an Fe2+-containing extradiol dioxygenase, no evidence for a superoxo or peroxo intermediate preceding the alkylperoxo was found. This observation and the lack of spectroscopic evidence for an Fe2+ intermediate that could bind O2 are consistent with concerted formation of the alkylperoxo followed by Criegee rearrangement to yield the anhydride and ultimately ring-opened product. Structural comparison of the alkylperoxo intermediates from the intra- and extradiol dioxygenases provides a rationale for site specificity of ring cleavage.

scholarly journals Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a “Bridging Peroxo” Intermediate Involved in Facile 4e–/4H+ O2-Reduction

2015 ◽  
Vol 137 (40) ◽  
pp. 12897-12905 ◽  
Author(s):  
Sudipta Chatterjee ◽  
Kushal Sengupta ◽  
Shabnam Hematian ◽  
Kenneth D. Karlin ◽  
Abhishek Dey
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
O2 Reduction ◽  
Peroxo Intermediate
Sign in / Sign up

Export Citation Format

Share Document