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The oxidant‐responsive diaphorase of Rhodobacter capsulatus is a ferredoxin (flavodoxin)‐NADP(H) reductase
Author(s) -
Bittel Cristian,
Tabares Leandro C.,
Armesto Martín,
Carrillo Néstor,
Cortez Néstor
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01075-5
Subject(s) - flavodoxin , rhodobacter , ferredoxin , flavoprotein , ferredoxin—nadp(+) reductase , biochemistry , reductase , diaphorase , chemistry , biology , enzyme , mutant , gene
Challenge of Rhodobacter capsulatus cells with the superoxide propagator methyl viologen resulted in the induction of a diaphorase activity identified as a member of the ferredoxin (flavodoxin)‐(reduced) nicotinamide adenine dinucleotide phosphate (NADP(H)) reductase (FPR) family by N‐terminal sequencing. The gene coding for Rhodobacter FPR was cloned and expressed in Escherichia coli . Both native and recombinant forms of the enzyme were purified to homogeneity rendering monomeric products of ∼30 kDa with essentially the same spectroscopic and kinetic properties. They were able to bind and reduce Rhodobacter flavodoxin (NifF) and to mediate typical FPR activities such as the NADPH‐driven diaphorase and cytochrome c reductase.