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H2O2 and (.)NO scavenging by Mycobacterium leprae truncated hemoglobin O
Authors:Ascenzi Paolo  De Marinis Elisabetta  Coletta Massimo  Visca Paolo
Institution:a Department of Biology and Interdepartmental Laboratory for Electron Microscopy, University Roma Tre, Viale Guglielmo Marconi 446, I-00146 Roma, Italy
b National Institute for Infectious Diseases I.R.C.C.S. ‘Lazzaro Spallanzani’, Via Portuense 292, I-00149 Roma, Italy
c Department of Experimental Medicine and Biochemical Sciences, University of Roma ‘Tor Vergata’, Via Montpellier 1, I-00133 Roma, Italy
Abstract:Kinetics of ferric Mycobacterium leprae truncated hemoglobin O (trHbOsingle bondFe(III)) oxidation by H2O2 and of trHbOsingle bondFe(IV)double bond; length as m-dashO reduction by radical dotNO and NO2 are reported. The value of the second-order rate constant for H2O2-mediated oxidation of trHbOsingle bondFe(III) is 2.4 × 103 M−1 s−1. The value of the second-order rate constant for radical dotNO-mediated reduction of trHbOsingle bondFe(IV)double bond; length as m-dashO is 7.8 × 106 M−1 s−1. The value of the first-order rate constant for trHbOsingle bondFe(III)single bondONO decay to the resting form trHbOsingle bondFe(III) is 2.1 × 101 s−1. The value of the second-order rate constant for NO2-mediated reduction of trHbOsingle bondFe(IV)double bond; length as m-dashO is 3.1 × 103 M−1 s−1. As a whole, trHbOsingle bondFe(IV)double bond; length as m-dashO, generated upon reaction with H2O2, catalyzes radical dotNO reduction to NO2. In turn, radical dotNO and NO2 act as antioxidants of trHbOsingle bondFe(IV)double bond; length as m-dashO, which could be responsible for the oxidative damage of the mycobacterium. Therefore, Mycobacterium leprae trHbO could be involved in both H2O2 and radical dotNO scavenging, protecting from nitrosative and oxidative stress, and sustaining mycobacterial respiration.
Keywords:Fe(III)  ferric heme-protein  Fe(IV)double bond</a>  <a href=length as m-dash" src="http://cdn  els-cdn  O" target="_blank">com/sd/entities/dbnd" class="glyphImg">O  ferryl heme-protein  Fe(III)single bondels-cdn  ONO" target="_blank">com/sd/entities/sbnd" class="glyphImg">ONO  O-nitrito ferric heme-protein  Hb  hemoglobin  Lb  leghemoglobin  Mb  myoglobin  TrHbO  truncated Hb O
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