STRUCTURAL AND FUNCTIONAL MODELS OF THE DIMANGANESE CATALASE ENZYMES .2. STRUCTURE, ELECTROCHEMICAL, REDOX, AND EPR PROPERTIES

Catalysts which functionally mimic the bacterial dimanganese catalase enzymes have been synthesized and their structure, electrochemical, re dox, and EPR spectra have been compared to the enzyme. These compounds are formulated as [LMn(2)(II,II)X]Y-2,mu-X=CH3CO2, ClCH2CO2; Y=ClO4, BPh(4), CH3CO2, possessing a bridging mu-alkoxide from the ligand, HL = (2-methylenebenzimidazole)-1,3-diaminopropan-2-ol. An X-ray diffract ion structure of [LMn(2)(CH3CO2)(butanol)](ClO4)(2).H2O, in the monocl inic space group P2(1)/c, confirmed the anticipated N6O septadentate c oordination of the HL ligand, the bridging mu-acetate, and revealed bo th five- and six-coordinate Mn ions; the latter arising from a butanol solvent molecule. This contrasts with the six-coordinate Mn ions obse rved for the mu-Cl and mu-OH derivatives, LMn(2)Cl(3) and LMn(2)(OH)Br -2 (Mathur et al. J. Am. Chem. Soc. 1987, 109, 5227-5232). Like the en zyme, three electrons can be removed from these complexes to form four oxidation states ranging from Mn-2(II,II) to Mn-2(III,IV). Three of t hese have been characterized by EPR and found to possess electronic gr ound states, Mn-III electron orbital configurations, Mn-55 hyperfine p arameters, and Heisenberg exchange interactions analogous to those obs erved in the enzyme. For the mu-carboxylate derivatives electrochemist ry reveals the initial oxidation process involves loss of two electron s at 0.81-0.86 V, forming Mn-2(III,III), followed by dismutation to yi eld a Mn-2(II,III) and Mn-2(III,IV) species. By contrast, the mu-Cl an d mu-OH derivatives oxidize by an initial one-electron process (0.49-0 .54 V). For the mu-carboxylate derivatives chemical oxidation with Pb( OAc)(4) also reveals an initial two-electron oxidation to a Mn-2(III,I II) species, which dismutates to form both Mn-2(II,III) and Mn-2(III,I V) species. The two Mn-2(II,III) species formed by these methods exhib it Mn-55 hyperfine fields differing in magnitude by 9% (150 G), implyi ng different Mn coordination environments induced by the electrolyte. The different ligand coordination observed in the enzyme (predominantl y oxo and carboxylato) appears to be responsible for stabilization of the MnCat(III,III) oxidation state as the resting state.