Abstract.
The magnetic properties of the reduced catalase from Lactobacillus plantarum have been studied for the active enzyme and its fluoride complex through variable field/variable temperature magnetization measurements. The magnetic exchange interaction deduced from these experiments [fluoride complex: –J=1.3(1) cm–1; active enzyme: –J=5.6(5) cm–1; H=–2J S 1 S 2] are similar to those presently obtained in a re-analysis of the data for the corresponding forms of the Thermus thermophilus enzyme (previously published in 1997, Angew Chem Int Ed Engl 36:1626–1628): phosphate complex: –J=2.1(2) cm–1; active enzyme –J=5.0(3) cm–1. These results concur to a unified picture for the two enzymes, consistent with the presence of a hydroxide bridge in the reduced active catalases and its replacement by an aqua bridge in the anion-inhibited enzymes as the main mediators of the magnetic exchange.
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Le Pape, L., Perret, E., Michaud-Soret, I. et al. Magnetization studies of the active and fluoride-inhibited derivatives of the reduced catalase of Lactobacillus plantarum: toward a general picture of the anion-inhibited and active forms of the reduced dimanganese catalases. J Biol Inorg Chem 7, 445–450 (2002). https://doi.org/10.1007/s00775-001-0319-x
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DOI: https://doi.org/10.1007/s00775-001-0319-x