PubMed · 4143574
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D S Spence. 1971-12-11. Bromism.. https://doi.org/10.1016/s0140-6736(71)90651-9
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Hydrogen peroxide, which is a substrate of vanadium bromoperoxidase (V-BrPO), has been shown to be a noncompetitive inhibitor of V-BrPO. Hydrogen peroxide inhibition increases with increasing pH. The inhibition is reversible under the conditions of the initial steady-state kinetic experiments. Analysis of the inhibition constants (KiiH2O2, KisH2O2) versus H+ concentration indicates that an ionizable group with a pKa between 6.5 and 7 is involved in the inhibition. The origin of the oxygen atoms in the dioxygen produced by the V-BrPO-catalyzed bromide-assisted disproportionation of hydrogen peroxide has been shown through H2(18)O2 labeling experiments to originate from the same molecule of hydrogen peroxide. V-BrPO-catalyzed bromination is shown to be an electrophilic (Br+) as opposed to a radical (Br.) process. The stoichiometry of H2O2 consumed to MCD reacted or to O2 produced is reported. The concentration of hydrogen peroxide also affects the competition of dioxygen formation during MCD bromination; competitive dioxygen formation is strongly enhanced at high pH. Turnover of V-BrPO under conditions of very high hydrogen peroxide concentration leads to irreversible inactivation at pH 4 and pH 5. Much less inactivation occurs during turnover at long reaction times at higher pH (> pH 6), and the inactivation can be fully reversed by subsequent addition of vanadate.
Effect of gamma radiation on flavocytochrome b2 in dilute aqueous solution was studied. A study of the effect of the radiolytically produced inorganic free-radical anions such as I2.-, Br2.- and (SCN)2.- on the enzyme activity indicates the involvement of cysteine and tyrosine residues in the catalytic activity of flavocytochrome b2. The changes in kinetic parameters, i.e., Michaelis-Menten constant Km and maximal velocity Vmax, due to irradiation under different conditions suggest that radiation induced enzyme inactivation is the result of destruction of active-site residues as well as modification of the substrate binding site. Fluorescence studies of unirradiated and irradiated enzyme reveal that FMN (flavin mononucleotide) is inaccessible to water radicals.
Voltage-clamp experiments were performed on lipid bilayer membranes to study the voltage dependence of the iodine-mediated halide transport. Under all experimental conditions only one exponential current relaxation, apart from the capacitive spike, could be resolved up to a clamp voltage of 200 mV. The current relaxation could be described by an initial conductance, G0, the relaxation time constant, tau, and the relaxation amplitude, alpha, that is the difference between the initial current, I0, and the steady state current, I chi, divided by the steady state current. The occurrence of one single exponential relaxation suggested that one of the different transport steps involved in the carrier-mediated ion transport according to the Lüger-model is always in equilibrium. This is most probably the transport of the free carriers across the membrane. The voltage dependence of G0, tau, and of alpha were used to determine the voltage dependence of the translocation rate constants of the complexed carriers, kAS. In the case of the iodine-mediated iodide transport, G0, tau and alpha were only mediate voltage-dependent, which means the voltage dependent translocation of the complex encounters a trapezoidal barrier shape. For the iodine-mediated bromide translocation G0, tau and alpha exhibited no dependence on the applied clamp-voltage, which suggested that a square Nernst-Planck barrier limits the transport of the corresponding complex.