PMID: 6402017Jan 12, 1983Paper

The inhibition of rhodanese by lipoate and iron-sulfur proteins

Biochimica Et Biophysica Acta
Silvia PaganiP Cerletti

Abstract

A study was made on the effects of DL-dihydrolipoate, lipoate and iron-sulfur proteins on the activity of rhodanese (EC 2.8.1.1) with dihydrolipoate or cyanide as acceptors. DL-Dihydrolipoate inactivates rhodanese, lipoate does not, and the opposite occurs with the sulfur-free form of the transferase. The observed effects vary with the sulfane sulfur acceptor from rhodanese (i.e., dihydrolipoate or cyanide) and depend on intramolecular oxidation of the catalytic sulfhydryl or on formation of a mixed disulfide with dihydrolipoate. Thiosulfate protects against inactivation by reloading the active-site cysteine with persulfide sulfur. The inhibition of sulfur transfer by iron-sulfur proteins appears related to the amount of native iron-sulfur structure interacting with rhodanese. The implications of the results for a possible biological role of rhodanese are considered.

References

Apr 8, 1976·Biochimica Et Biophysica Acta·R D Baillie, P M Horowitz
Jan 3, 1977·European Journal of Biochemistry·F BonomiC Cannella
May 11, 1978·Nature·J H PloegmanJ Russell
Aug 12, 1976·Biochimica Et Biophysica Acta·L PecciC Cannella
Nov 3, 1975·Biochemical and Biophysical Research Communications·S K Kim, P M Horowitz
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May 1, 1959·Archives of Biochemistry and Biophysics·G L ELLMAN
Dec 1, 1964·Analytical Biochemistry·R F ITZHAKI, D M GILL

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Citations

Apr 12, 2001·European Journal of Biochemistry·S IamettiF Bonomi
Jul 16, 1984·European Journal of Biochemistry·S PaganiP Cerletti
Apr 1, 1985·European Journal of Biochemistry·F BonomiD M Kurtz
Apr 1, 1988·FEMS Microbiology Reviews·M Bruschi, F Guerlesquin

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