Reductive half-reaction of xanthine oxidase with xanthine. Observation of a spectral intermediate attributable to the molybdenum center in the reaction of enzyme with xanthine.

DOI: 10.1016/s0021-9258(18)54112-0 Authors: J.H. Kim, Russ Hille Abstract: The reductive half-reaction of xanthine oxidase with substoichiometric concentrations of xanthine and 1-methylxanthine at pH 10 and 8.5 has been examined by UV-visible stopped-flow and...

Mechanism of Assembly of the Dimanganese-Tyrosyl Radical Cofactor of Class Ib Ribonucleotide Reductase: Enzymatic Generation of Superoxide Is Required for Tyrosine Oxidation via a Mn(III)Mn(IV) Intermediate

DOI: 10.1021/ja312457t Authors: Joseph A. Cotruvo, Troy A. Stich, R. David Britt, JoAnne Stubbe Abstract: Ribonucleotide reductases (RNRs) utilize radical chemistry to reduce nucleotides to deoxynucleotides in all organisms. In the class Ia and Ib RNRs, this reaction...

The pathway of electrons through QH2:cytochrome c oxidoreductase studied by pre-steady-state kinetics

DOI: 10.1016/0005-2728(82)90276-6 Authors: S. de Vries, Simon P. J. Albracht, J.A. Berden, E.C. Slater Abstract: N/A

Insights in the mechanism of selective olefin oligomerisation catalysis using stopped-flow freeze-quench techniques: A Mo K-edge QEXAFS study

DOI: 10.1016/j.jcat.2011.10.015 Authors: Stuart A. Bartlett, Peter P. Wells, Maarten Nachtegaal, Andrew J. Dent, Giannantonio Cibin, Gillian Reid, John Evans, Moniek Tromp Abstract: N/A

Kinetic analysis of amino acid radicals formed in H ₂ O ₂ -driven Cu ^I LPMO reoxidation implicates dominant homolytic reactivity

DOI: 10.1073/pnas.1922499117 Authors: Stephen M. Jones, Wesley J. Transue, Katlyn K. Meier, Bradley R. Kelemen, Edward I. Solomon Abstract: Lytic polysaccharide monooxygenases (LPMOs) have been proposed to react with both [Formula: see text] and [Formula: see text] as...

Cobamides and Ribonucleotide Reduction

DOI: 10.1016/s0021-9258(19)42735-x Authors: William H. Orme‐Johnson, Helmut Beinert, Raymond L. Blakley Abstract: Abstract Reaction mixtures containing coenzyme B12 (5′-deoxyadenosylcobalamin), an equivalent concentration of ribonucleotide reductase from...

An Oxyferrous Heme/Protein-based Radical Intermediate Is Catalytically Competent in the Catalase Reaction of Mycobacterium tuberculosis Catalase-Peroxidase (KatG)

DOI: 10.1074/jbc.m808106200 Authors: Javier Suárez, Kalina Ranguelova, Andrzej A. Jarzęcki, J. Manzerova, Vladimir Krymov, Xiangbo Zhao, Shengwei Yu, Leonid Metlitsky, Gary J. Gerfen, Richard S. Magliozzo Abstract: A mechanism accounting for the robust catalase...

Direct Spectroscopic and Kinetic Evidence for the Involvement of a Peroxodiferric Intermediate during the Ferroxidase Reaction in Fast Ferritin Mineralization

DOI: 10.1021/bi980847w Authors: Alice S. Pereira, William Small, Carsten Krebs, Pedro Tavares, Dale E. Edmondson, Elizabeth C. Theil, Boi Hanh Huynh Abstract: Rapid freeze-quench (RFQ) Mössbauer and stopped-flow absorption spectroscopy were used to monitor the...

The Ferroxidase Reaction of Ferritin Reveals a Diferric μ-1,2 Bridging Peroxide Intermediate in Common with Other O₂-Activating Non-Heme Diiron Proteins

DOI: 10.1021/bi990095l Authors: Pierre Moënne‐Loccoz, Carsten Krebs, Kara Herlihy, Dale E. Edmondson, Elizabeth C. Theil, Boi Hanh Huynh, Thomas M. Loehr Abstract: Ferritins are ubiquitous proteins that concentrate, store, and detoxify intracellular iron through...

Probing the Reaction Mechanism of the d-ala-d-ala Dipeptidase, VanX, by Using Stopped-Flow Kinetic and Rapid-Freeze Quench EPR Studies on the Co(II)-Substituted Enzyme

DOI: 10.1021/ja0627343 Authors: Megan L. Matthews, Gopalraj Periyannan, Christine E. Hajdin, Tara K. Sidgel, Brian Bennett, Michael W. Crowder Abstract: In an effort to probe the reaction mechanism of VanX, the d-ala-d-ala dipeptidase required for high-level...