Detection of a Tryptophan Radical as an Intermediate Species in the Reaction of Horseradish Peroxidase Mutant (Phe-221 → Trp) and Hydrogen Peroxide

DOI: 10.1074/jbc.273.24.14753 Authors: Atsushi Morimoto, Motomasa Tanaka, Satoshi Takahashi, Koichiro Ishimori, Hiroshi Hori, Isao Morishima Abstract: The crucial reaction intermediate in the reaction of peroxidase with hydrogen peroxide (H2O2), compound I, contains a...

Spectroscopic evidence for the role of a site of the di-iron catalytic center of ferritins in tuning the kinetics of Fe( ii ) oxidation

DOI: 10.1039/c6mb00235h Authors: Kourosh Honarmand Ebrahimi, Eckhard Bill, Peter‐Leon Hagedoorn, Wilfred R. Hagen Abstract: Ferritin is a nanocage protein made of 24 subunits. Its major role is to manage intracellular concentrations of free Fe(ii) and Fe(iii) ions,...

Mechanistic Analysis of Stereodivergent Nitroalkane Cyclopropanation Catalyzed by Nonheme Iron Enzymes

DOI: 10.1021/jacs.3c08413 Authors: Richiro Ushimaru, Lide Cha, Shotaro Shimo, Xiaojun Li, Jared C. Paris, Takahiro Mori, Kazunori Miyamoto, Lindsay Coffer, Masanobu Uchiyama, Yisong Guo, Wei‐chen Chang, Ikuro Abe Abstract: BelL and HrmJ are α-ketoglutarate-dependent...

Activation of [CrCl₃{PPh₂N(ⁱPr)PPh₂}] for the selective oligomerisation of ethene: a Cr K-edge XAFS study

DOI: 10.1039/c6cy00902f Authors: Stuart A. Bartlett, Jerome Moulin, Moniek Tromp, Gillian Reid, A. J. Dent, Giannantonio Cibin, David S. McGuinness, John Evans Abstract: Freeze-quench XAFS reveals initial methylation of the Cr(iii) precursor prior to reduction to...

Functionality of the Three-Site Ferroxidase Center of Escherichia coli Bacterial Ferritin (EcFtnA)

DOI: 10.1021/bi401517f Authors: Fadi Bou‐Abdallah, Heiko Yang, A. Awomolo, Bret Cooper, Mark Woodhall, Simon C. Andrews, N. Dennis Chasteen Abstract: At least three ferritins are found in the bacterium Escherichia coli: the heme-containing bacterioferritin (EcBFR) and...

Mapping the Initial Stages of a Protective Pathway that Enhances Catalytic Turnover by a Lytic Polysaccharide Monooxygenase

DOI: 10.1021/jacs.3c06607 Authors: Jingming Zhao, Ying Zhuo, Daniel E. Díaz, Muralidharan Shanmugam, Abbey Telfer, Peter J. Lindley, Daniel Kracher, Takahiro Hayashi, Lisa S. Seibt, Florence J. Hardy, Oliver Manners, Tobias M. Hedison, Katherine A. Hollywood, Reynard...

The Kinetic Reaction Mechanism of the Vibrio cholerae Sodium-dependent NADH Dehydrogenase

DOI: 10.1074/jbc.m115.658773 Authors: Karina Tuz, Katherine G. Mezic, Tianhao Xu, Blanca Barquera, Oscar Juárez Abstract: The sodium-dependent NADH dehydrogenase (Na(+)-NQR) is the main ion transporter in Vibrio cholerae. Its activity is linked to the operation of the...

Advanced X-ray absorption spectroscopy : Analyzing electronic structures of catalysts

DOI: OA:W3021031383 Authors: Jean‐Pierre H. Oudsen Abstract: In catalysis, it is important to know the exact structure of the catalyst, especially under catalytic conditions. Spectroscopic information on the catalyst is crucial to reveal for example structure-activity...

The Reaction of Trimethylamine Dehydrogenase with Trimethylamine

DOI: 10.1074/jbc.274.19.13147 Authors: Mei-Huei Jang, Jaswir Basran, Nigel S. Scrutton, Russ Hille Abstract: The reductive half-reaction of trimethylamine dehydrogenase has been studied using the substrate diethylmethylamine over the pH range 6-10. It is found that...

Detection, identification, and quantification of oxidative protein modifications

DOI: 10.1074/jbc.rev119.006217 Authors: Clare L. Hawkins, Michael J. Davies Abstract: Exposure of biological molecules to oxidants is inevitable and therefore commonplace. Oxidative stress in cells arises from both external agents and endogenous processes that...