PMID:18286376: Difference between revisions

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<span style = 'font-size: large'> '''Boxhammer, S, Glaser, S, Kühl, A, Wagner, AK and Schmidt, CL'''  (2008) Characterization of the recombinant Rieske [2Fe-2S] proteins HcaC and YeaW from E. coli.''Biometals'' '''21''':459-67</span>
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|{{TableHeadingColor}} |'''Abstract''' || <protect>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.</protect>
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'''No author listed''' (2008) Characterization of the recombinant Rieske [2Fe-2S] proteins HcaC and YeaW from E. coli. ''Biometals'' '''21''':459-67
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!align=left  |Abstract
*  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18286376 PubMed]
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18286376 PubMed]
Online version:[http://dx.doi.org/10.1007/s10534-008-9134-y 10.1007/s10534-008-9134-y]
Online version:[http://dx.doi.org/10.1007/s10534-008-9134-y 10.1007/s10534-008-9134-y]
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!align=left  |Keywords
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Amino Acid Sequence; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/classification; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Ferredoxins/chemistry; Ferredoxins/classification; Ferredoxins/genetics; Ferredoxins/metabolism; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/classification; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Oxidoreductases/chemistry; Oxidoreductases/classification; Oxidoreductases/genetics; Oxidoreductases/metabolism; Phylogeny; Protein Structure, Tertiary; Recombinant Proteins/chemistry; Recombinant Proteins/classification; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Alignment; Sequence Analysis, Protein
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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{{LitSignificance}}

Revision as of 19:04, 1 September 2013

Citation

No author listed (2008) Characterization of the recombinant Rieske [2Fe-2S] proteins HcaC and YeaW from E. coli. Biometals 21:459-67

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.

Links

PubMed Online version:10.1007/s10534-008-9134-y

Keywords

Amino Acid Sequence; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/classification; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Ferredoxins/chemistry; Ferredoxins/classification; Ferredoxins/genetics; Ferredoxins/metabolism; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/classification; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Oxidoreductases/chemistry; Oxidoreductases/classification; Oxidoreductases/genetics; Oxidoreductases/metabolism; Phylogeny; Protein Structure, Tertiary; Recombinant Proteins/chemistry; Recombinant Proteins/classification; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Alignment; Sequence Analysis, Protein

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