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.

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=-2 J 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.