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C) Nitrite reductase activity of XOR as exhibited by the substrate(xanthine)-reduced enzyme. Electrons derived from xanthine are not passed to other redox centers but to nitrite (NO2À), which is thereby reduced to nitric oxide (•NO). This activity is strictly dependent on low-oxygen conditions. (d) Nitrite reductase activity of XOR after reduction of the enzyme by NADH. This activity involves all four redox-active groups and resembles the inverse reaction of (a) with regard to electron flow. It is assumed that this activity also occurs in the presence of O2.
6 Schematic presentation of interconversion of mammalian xanthine oxidoreductase into dehydrogenase and oxidase forms. Mammalian XOR is converted from the initially existing dehydrogenase form (middle) into the oxidase form either irreversibly by limited proteolysis within the hinge regions between the domains (right) or reversibly by oxidation of conserved cysteine thiols (left). For clarity, only one monomer of the otherwise homodimeric enzyme is presented Established and Proposed Roles of Xanthine Oxidoreductase in Oxidative and.
Sp. tritici infection. Plant Sci 87:225–231 Montalbini P (1995) Effect of rust infection on purine catabolism enzyme levels in wheat leaves. Physiol Mol Plant Pathol 46:275–292 Montalbini P (1998) Purification and some properties of xanthine dehydrogenase from wheat leaves. Plant Sci 134:89–102 Montalbini P (2000) Xanthine dehydrogenase from leaves of leguminous plants: purification, characterization and properties of the enzyme. J Plant Physiol 156:3–16 Montalbini P, Della Torre G (1996) Evidence of a two-fold mechanism responsible for the inhibition by allopurinol of the hypersensitive response induced in tobacco by tobacco necrosis virus.