82247-40-3Relevant academic research and scientific papers
Cytochrome Oxidase Models. 3. Spin Coupling across Imidazolate Bridges in Binuclear Metalloporphyrin Complexes of Iron and Copper
Dessens, Steven E.,Merrill, Connie L.,Saxton, Robert J.,Ilaria, Robert L.,Lindsey, John W.,Wilson, Lon J.
, p. 4357 - 4361 (1982)
Four new μ-imidazolato binuclear metalloporphyrin compounds of FeIII and CuII or ZnII have been synthesized, isolated, and characterized in the solid state as a model systems for the active of cytochrome c oxidase.The compounds have been derived from III(TPP)X> (X = Cl- or OSO2CF3-) and II(imidH)2DAP>2+ (M = Zn or Cu) to yield species containing the following μ-imidazolato cationic cores: III(imid)ZnII>+ (1), III(imid)CuII>+ (2), III(imid)ZnII>+ (3), and III(imid)CuII>+ (4).Comparative magnetochemical (15 300 K), Moessbauer (100 K), and EPR (10 K) studies of 1 and 2 are consistent with essentially identical electronic environments about FeIII (S = 1/2) with -JFeIII-CuII -1 in 2.Similar comparative studies of 3 and 4 are somewhat complicated by the presence of what appears to be two distinct molecular species of S = 5/2 and 1/2 coexisting in the same crystalline sample.The magnetic properties and silent EPr behavior of 4 have been rationalized in terms of a (S = 0, 2) mixture arising from strong antiferromagnetic coupling between FeIII (S = 1/2, 5/2) and CuII (S = 1/2), where -JFeIII-CuII >/ca. 200 cm-1.The implication of this result to the possible active-site structure of oxidase has been briefly considered.
