@article {Folgosa:2011kf,
	title = {{New spectroscopic and electrochemical insights on a class I superoxide reductase: Evidence for an intramolecular electron transfer pathway.}},
	journal = {Biochemical Journal},
	year = {2011},
	abstract = {Superoxide reductases are enzymes involved in bacterial resistance to reactive oxygen species, catalyzing the reduction of superoxide anions to hydrogen peroxide. So far three structural classes have been identified. Class I enzymes have two iron-center containing domains. Most studies have been focused on the catalytic iron site (center II), but the role of center I is yet poorly understood. The possible roles of this iron site were approached by an integrated study using both classical and fast kinetics measurements as well as direct electrochemistry. A new heterometallic form of the protein with a zinc-substituted center I, maintaining the iron active site center II was obtained, resulting in a stable derivative useful for comparison with the native all-iron from. Second order rate constants for the electron transfer between reduced rubredoxin and the different SOR forms were determined to be 2.8x107 (M-1s-1) and 1.3x106 (M-1s-1) for SORFe(IIII)-Fe(II) and for SORFe(IIII)-Fe(III) forms respectively, and 3.2x106 (M-1s-1) for the SORZn(II)-Fe(III) form. The results obtained seem to indicate that center I transfers electrons from the putative physiologic donor, rubredoxin, to the catalytic active iron site (intramolecular process). In addition, electrochemical results show that conformational changes are associated to the redox state of center I, which may enable a faster catalytic response towards superoxide anion. The apparent rate constants calculated for the SOR-mediated electron transfer also support this observation.},
	doi = {10.1042/BJ20110836},
	author = {Folgosa, Filipe and Cordas, Cristina M and Santos, Joana A and Pereira, Alice S. and Moura, Jose J. G. and Tavares, Pedro Ant{\'o}nio Brito and Moura, Isabel}
}
