Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis

DOI: 10.1042/bj1690361 Authors: Daniël J. Steenkamp, Thomas P. Singer Abstract: Bacterial trimethylamine dehydrogenase contains a novel type of covalently bound flavin mononucleotide and a tetrameric iron-sulphur centre. The dehydrogenase takes up 1.5mol of...

Chemical Nature and Reaction Mechanisms of the Molybdenum Cofactor of Xanthine Oxidoreductase

DOI: 10.2174/1381612811319140010 Authors: Ken Okamoto, Teruo Kusano, Takeshi Nishino Abstract: Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions...

Vibrational analyses of the reaction of oxymyoglobin with NO using a photolabile caged NO donor at cryogenic temperatures

DOI: 10.1016/j.jinorgbio.2024.112633 Authors: Therese Albert, A. VInay Kumar, Jonathan D. Caranto, Pierre Moënne‐Loccoz Abstract: N/A

Evaluation of research and development: Methods for evaluating the results of European community R & D programmes

DOI: 10.1016/0377-2217(83)90273-4 Authors: Alok Chakrabarti Abstract: N/A

Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase

DOI: 10.1073/pnas.0604005103 Authors: Lee M. Hoffart, Eric W. Barr, Robert B. Guyer, J. Martin Bollinger, Carsten Krebs Abstract: The Fe(II)- and alpha-ketoglutarate (alphaKG)-dependent dioxygenases use mononuclear nonheme iron centers to effect hydroxylation of their...