NDLI: Characterization of the recombinant Rieske [2Fe–2S] proteins HcaC and YeaW from E. coli

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Characterization of the recombinant Rieske [2Fe–2S] proteins HcaC and YeaW from E. coli

Content Provider	Springer Nature Link
Author	Boxhammer, S. Glaser, S. Kühl, A. Wagner, A. K. Schmidt, Christian L.
Copyright Year	2008
Abstract	Three genes within the genome of E. coli K12 are predicted to encode proteins containing the typical Rieske iron–sulfur cluster-binding motifs. Two of these, hcaC and yeaW, were overexpressed in E. coli BL21 and Tuner (DE3) pLacI. The recombinant proteins were purified and analyzed by UV/Vis- and EPR-spectroscopy. HcaC and YeaW display the typical redox-dependent UV/Vis-spectra of iron–sulfur proteins. The EPR spectrum of reduced HcaC shows characteristic g-values of a Rieske cluster whereas the g-values for YeaW are close to the upper limit for this type of iron–sulfur cluster. Both iron–sulfur clusters could be reduced by dithionite, but not by ascorbate, confirming their classification as low-potential Rieske proteins as derived from the amino acid sequences. A phylogenetic analysis of the two proteins reveals that HcaC clearly segregates with the Rieske ferredoxins of class IIB oxygenases whereas the classification of YeaW remains doubtful.
Starting Page	459
Ending Page	467
Page Count	9
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	21
Issue Number	4
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2008-02-20
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	E. coli Low-potential Rieske iron–sulfur protein Phenylpropionic acids Phylogenetic analysis Physical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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