The tetra-nuclear title compound, [Cu(2)Ti(2)(C(6)H(6)NO(6))(2)O(O(2))(2)(H(2)O)(10)]·7H(2)O, lies about a twofold rotation axis that passes through the bridging oxide atom. The titanium atom is N,O,O',O''-chelated by the nitrilo-triacetate and O,O'-chelated by the peroidxo group and is coordinated to the bridging O atom in an overall penta-gonal-bipyramidal geometry. The O atom of one of the c...

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The first dimeric catalase-peroxidase of eucaryotic origin, an intracellular hydroperoxidase from Penicillium simplicissimum which exhibited both catalase and peroxidase activities, has been isolated. The enzyme has an apparent molecular mass of about 170 kDa and is composed of two identical subunits. The purified protein has a pH optimum for catalase activity at 6.4 and for peroxidase at 5.4. ...

Peroxidase catalyzes oxidatic reactions (in which oxygen is the electron acceptor) as well as the classic peroxidatic reactions (in which hydrogen peroxide is the electron acceptor) (4, 10). There is considerable evidence that the enzyme which catalyzes the oxidatic degradation of the plant growth hormone, indole-3acetic acid, is a peroxidase (8). Recently Yang (12, 13) and Ku et al. (5) have d...

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In the title complex, [Pr(2)(C(2)O(4))(3)(H(2)O)(4)](n), the two independent Pr(III) ions are both nine-coordinated in a distorted monocapped square-anti-prismatic geometry by seven O atoms from four oxalate ligands and two water mol-ecules. The Pr(III) ions are bridged by the oxalate ligands, forming a layer parallel to (001). O-H⋯O hydrogen bonds connect the layers.