In strict or facultative anaerobic microorganisms, the flavodiiron proteins (FDP) have been recognized to take part in the response mechanism to both nitrosative and oxidative stress. Their function consists of the reduction of nitric oxide and/or oxygen at the diiron center, and specificity for one substrate or the other appears to be characteristic of the corresponding microorganism, possibly depending on the properties of the catalytic site. Particularly focused on the flavorubredoxin, i.e., the Escherichia coli FDP, herein the amperometric and time-resolved spectroscopic approaches are presented, giving access to the study of in vitro reactivity of a complex multi-redox center enzyme.
Kinetic characterization of the Escherichia coli nitric oxide reductase flavorubredoxin / Vicente, Jb; Francesca M., Scandurra; Forte, Elena; Brunori, Maurizio; Sarti, Paolo; Miguel, Teixeira; Giuffre', Alessandro. - 437:(2008), pp. 47-62. [10.1016/s0076-6879(07)37003-1]
Kinetic characterization of the Escherichia coli nitric oxide reductase flavorubredoxin
FORTE, Elena;BRUNORI, Maurizio;SARTI, Paolo;GIUFFRE', ALESSANDRO
2008
Abstract
In strict or facultative anaerobic microorganisms, the flavodiiron proteins (FDP) have been recognized to take part in the response mechanism to both nitrosative and oxidative stress. Their function consists of the reduction of nitric oxide and/or oxygen at the diiron center, and specificity for one substrate or the other appears to be characteristic of the corresponding microorganism, possibly depending on the properties of the catalytic site. Particularly focused on the flavorubredoxin, i.e., the Escherichia coli FDP, herein the amperometric and time-resolved spectroscopic approaches are presented, giving access to the study of in vitro reactivity of a complex multi-redox center enzyme.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.