Abstract:
:The Fe(III) reductase activity was studied in the South African Fe(III)-reducing bacterium, Thermus scotoductus (SA-01). Fractionation studies revealed that the membrane as well as the soluble fraction contained NAD(P)H-dependent Fe(III) reductase activity. The membrane-associated enzyme was solubilized by KCl treatment and purified to electrophoretic homogeneity by hydrophobic interaction chromatography. A combination of ion-exchange and gel filtration chromatography was used to purify the soluble enzyme to apparent homogeneity. The molecular mass of the membrane-associated Fe(III) reductase was estimated to be 49 kDa, whereas the soluble Fe(III) reductase had an apparent molecular mass of 37 kDa. Optimum activity for the membrane-associated enzyme was observed at around 75 degrees C, whereas the soluble enzyme exhibited a temperature optimum at 60 degrees C.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Möller C,van Heerden Edoi
10.1111/j.1574-6968.2006.00499.xsubject
Has Abstractpub_date
2006-12-01 00:00:00pages
237-43issue
2eissn
0378-1097issn
1574-6968pii
FML499journal_volume
265pub_type
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