Structure of coproheme decarboxylase from Listeria monocytogenes during turnover
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Structure of coproheme decarboxylase from Listeria monocytogenes during turnover Descriptor: (4S)-2-METHYL-2,4-PENTANEDIOL, 1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC ACID FERROUS COMPLEX, Putative heme-dependent peroxidase lmo2113, ... Authors: Hofbauer, S, Pfanzagl, V, Mlynek, G, Puehringer, D. Deposit date: 2018-03-09 Release date: 2019-07-10 Last modified: 2024-01-17 Method: X-RAY DIFFRACTION (1.69 Å) Cite: Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Hemeb. Acs Catalysis, 9, 2019
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2018-03-09
