Expression, purification, and characterization of a [Fe2S2] cluster containing ferredoxin from Acidithiobacillus ferrooxidans.

Abstract:

:The [2Fe-2S] cluster containing ferredoxin has attracted much attention in recent years. Genetic analyses show that it has an essential role in the maturation of various iron-sulfur (Fe-S) proteins and functions as a component of the complex machinery responsible for the biogenesis of Fe-S clusters. The gene of ferredoxin from A. ferrooxidans ATCC 23270 was cloned, successfully expressed in Escherichia coli, and purified by one-step affinity chromatography to homogeneity. The MALDI-TOF MS and spectra results of the recombinant protein confirmed that the iron-sulfur cluster was correctly inserted into the active site of the protein. Site-directed mutagenesis results revealed that Cys42, Cys48, Cys51, and Cys87 were ligating with the [Fe(2)S(2)] cluster of the protein.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Zeng J,Huang X,Liu Y,Liu J,Qiu G

doi

10.1007/s00284-007-9025-4

subject

Has Abstract

pub_date

2007-12-01 00:00:00

pages

518-23

issue

6

eissn

0343-8651

issn

1432-0991

journal_volume

55

pub_type

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