The oxidant-responsive diaphorase of Rhodobacter capsulatus is a ferredoxin (flavodoxin)-NADP(H) reductase.

Abstract:

: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 approximately 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bittel C,Tabares LC,Armesto M,Carrillo N,Cortez N

doi

10.1016/s0014-5793(03)01075-5

keywords:

subject

Has Abstract

pub_date

2003-10-23 00:00:00

pages

408-12

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014579303010755

journal_volume

553

pub_type

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