TY - JOUR PY - 1993// TI - tBOOH Acts as a Suicide Substrate for Catalase JO - Archives of biochemistry and biophysics A1 - Pichorner, H. A1 - Jessner, G. A1 - Ebermann, R. SP - 258 EP - 264 VL - 300 IS - 1 N2 - The effects of t-butyl hydroperoxide (tBOOH) on bovine liver catalase were investigated. tBOOH is accepted as a substrate of catalase and in the absence of hydrogen donors leads to a destruction of the enzyme via compound II formation. During the decomposition of this enzyme-substrate complex catalase serves as internal hydrogen donor which results in destruction of the enzyme. Evidence for this destruction is given by: - a decrease of the Soret band in the uv/vis spectrum, - iron release from the enzyme, - decrease of the catalatic activity of the enzyme measured by oxygen release from hydrogen peroxide. Hydrogen donors like NADH and o-dianisidine have been found to protect the enzyme from destruction by tBOOH but lead to a structural alteration of the enzyme, shown by alteration of the electrophoretic mobility. In the presence of the hydrogen donor tBOOH is completely reduced to t-butanol, which is thought to proceed in a peroxidase-like reaction. © 1993 Academic Press, Inc.
Language: en
LA - en SN - 0003-9861 UR - http://dx.doi.org/10.1006/abbi.1993.1036 ID - ref1 ER -