Document Detail

[2Fe-2S] proteins in chlorosomes: redox properties of CsmI, CsmJ, and CsmX of the chlorosome envelope of Chlorobaculum tepidum.
MedLine Citation:
PMID:  23368794     Owner:  NLM     Status:  Publisher    
The chlorosome envelope of Chlorobaculum tepidum contains 10 polypeptides, three of which, CsmI, CsmJ, and CsmX, have an adrenodoxin-like domain harboring a single [2Fe-2S] cluster. Mutants were constructed that produced chlorosomes containing two, one, or none of these Fe/S proteins (Li et al., Biochemistry, 2012, accompanying paper). The EPR spectra, g-values, and linewidths of the Fe/S clusters in individual CsmI, CsmJ and CsmX proteins were obtained from studies with isolated chlorosomes. The Fe/S clusters in these proteins were characterized by EPR and could be differentiated on the basis of their g-values and linewidths. The EPR spectrum of wild-type chlorosomes could be simulated by a 1:1 admixture of the CsmI and CsmJ spectra. No contribution of CsmX to the EPR spectrum of chlorosomes was observed because of its low abundance. In chlorosomes that contained only CsmI or CsmJ, the midpoint potentials of the [2Fe-2S] clusters were -205 mV and +8 mV, respectively; the midpoint potential of the [2Fe-2S] cluster in CsmX was estimated to be more oxidizing than -180 mV. In wild-type chlorosomes the midpoint potentials of the [2Fe-2S] clusters were -348 mV for CsmI and +92 mV for CsmJ. The lower potential for CsmI in the presence of CsmJ, and the higher potential for CsmJ in the presence of CsmI, were attributed to interactions that occur when these proteins form complexes in the chlorosome envelope. The redox properties of the CsmI and CsmJ are consistent with their proposed participation in electron transfer to and from quenchers of energy transfer in chlorosomes.
T Wade Johnson; Hui Li; Niels-Ulrik Frigaard; John Harvey Golbeck; Donald A Bryant
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-31
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-2-1     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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