PMID: 9531477Jun 11, 1998Paper

pH-dependent inhibition by azide and fluoride of the iron superoxide dismutase from Propionibacterium shermanii

The Biochemical Journal
B MeierF Parak

Abstract

The iron-containing superoxide dismutase from Propionibacterium shermanii shows, in contrast with other iron superoxide dismutases, only a minor inhibition by azide or fluoride (10-100 mM) of up to 23% at pH 7.8. The activity of the protein with Mn bound to the active site was not diminished under the same conditions. The binding constant between azide and the Fe3+ ion was determined as approx. 2 mM and for fluoride approx. 2.3 mM; they are so far comparable to those known for other iron superoxide dismutases. This seems to be a discrepancy because all other iron superoxide dismutases so far known are described as being inhibited by 50-70% by 10 mM azide. However, towards lower pH there was a drastically increased inhibition by both anions. At pH 6.8 about 80% inhibition was exhibited by azide or fluoride at a concentration of 10 mM or higher. In contrast, on increasing the pH, azide or fluoride still bound to the Fe3+ at the active site but their inhibition capacity decreased. This observation implies that both anions bind to the metal at a position that is empty at low pH, whereas at higher pH water or a negatively charged hydroxyl anion is bound. It is likely that the superoxide anion binds to the same position and has to re...Continue Reading

Citations

Aug 21, 2012·Antioxidants & Redox Signaling·V Ashutosh Rao
Jan 29, 2008·Rapid Communications in Mass Spectrometry : RCM·Narciso CoutoM Filomena Duarte
Dec 31, 2003·The Journal of Biological Chemistry·Armand W J W TepperGerard W Canters
Feb 15, 2003·FEMS Microbiology Reviews·Robert E MarquisMarilaine Mota-Meira
Feb 28, 2002·The Journal of Biological Chemistry·Visith ThongboonkerdR J Doyle
Jan 19, 2000·Clinical Biochemistry·J M MatésI Núñez de Castro
Apr 19, 2008·Solid State Nuclear Magnetic Resonance·Th EmmlerG Buntkowsky

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