Evidence for non-cysteinyl coordination of the [2Fe-2S] cluster inEscherichia colisuccinate dehydrogenase-Reference-Cited by-同舟云学术

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Evidence for non-cysteinyl coordination of the [2Fe-2S] cluster inEscherichia colisuccinate dehydrogenase

Published:1992-03-02 Issue:1 Volume:299 Page:1-4
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Werth Mark T.,Sices Harry,Cecchini Gary,Schröder Imke,Lasage Susanne,Gunsalus Robert P.,Johnson Michael K.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80086-V/fullpdf

Reference14 articles.

1. Structure of the Succinate-Ubiquinone Oxidoreductase (Complex II)

2. B.A.C. Ackrell M.K. Johnson R.P. Gunsalus G. Cecchini F. Muller Chemistry and Biochemistry of Flavoenzymes III 1991 CRC Presss Boca Raton 229 297

3. Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster.

4. Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli

5. The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex.

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