Ferredoxins  are a group of iron-sulfur proteins which mediate electron
transfer in a wide variety of metabolic reactions. Ferredoxins can be divided
into several subgroups depending upon the physiological nature of the iron
sulfur cluster(s) and according to sequence similarities. One family of
ferredoxins groups together the following proteins that all bind a single 2Fe-2S iron-sulfur cluster:
Adrenodoxin (ADX) (adrenal ferredoxin), a vertebrate mitochondrial protein
which transfers electrons from adrenodoxin reductase to cytochrome P450scc,
which is involved in cholesterol side chain cleavage.
Putidaredoxin (PTX), a Pseudomonas putida protein which transfers electrons
from putidaredoxin reductase to cytochrome P450-cam, which is involved in
the oxidation of camphor.
Terpredoxin , a Pseudomonas protein which transfers electrons from
terpredoxin reductase to cytochrome P450-terp, which is involved in the
oxidation of α-terpineol.
Rhodocoxin , a Rhodococcus protein which transfers electrons from
rhodocoxin reductase to cytochrome CYP116 (thcB), which is involved in the
degradation of thiocarbamate herbicides.
Escherichia coli ferredoxin (gene fdx)  whose exact function is not yet
Rhodobacter capsulatus ferredoxin VI , which may transfer electrons to a
yet uncharacterized oxygenase.
In these proteins, four cysteine residues bind the iron-sulfur cluster. Three
of these cysteines are clustered together in the same region of the protein.
Our signature pattern spans that iron-sulfur binding region.
Nagy I. Schoofs G. Compernolle F. Proost P. Vanderleyden J. de Mot R.
Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase.
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