Active site chemistry of lysyl oxidase |
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| Authors: | K Govindaraju B U Nair T Ramasami D Ramaswamy |
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| Affiliation: | 1. Dept of Pharmacological and Biomolecular Sciences, Università degli Studi di Milano, 20134 Milan, Italy;2. IRCCS Multimedica Hospital, Sesto San Giovanni, 20099 Milan, Italy;3. Centro SISA per lo studio dell''Aterosclerosi, Ospedale Bassini, 20092 Cinisello Balsamo, Italy;1. Food Engineering and Technology Department, Institute of Chemical Technology, Matunga, Mumbai, 400 019, India;2. Institute of Chemical Technology, Marathwada Campus, Jalna, 431 213, India |
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| Abstract: | The bimolecular reduction of the Cu(II)-based enzyme lysyl oxidase with two inorganic reductants, tris bipyridylchromium(II) and (1,3,6,8,10,13,16,19)-octaazabicyclo (6,6,6)eicosanecobalt(II) has been examined at various ionic strength and [H+] conditions. The electrochemical properties of the enzyme have also been examined. The results show that Cu(II) is the redox site in the enzyme and has E 1/2 = 0.05 +/- 0.005 V against SCE. The observed rate constants, kobs, for the reduction of the enzyme by either Cr(bpy)32+ or Co(sep)2+ at any concentration of the reductant increased with the ionic strength of the medium. The ionic strength dependence of kobs has been analyzed in terms of the charge of the active site being 1 +. |
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