Characterization of the binding of Fe(III) to F1ATPase from bovine heart mitochondria

FEBS Letters
G LippeI Mavelli

Abstract

The binding Fe(III) to F1ATPase purified from beef heart mitochondria has been characterized by chemical analyses and EPR spectroscopy. F1ATPase binds 2 mol of Fe(III)/mol of protein selectively in the presence of saturating concentrations of ATP. In the absence of nucleotides or in the presence of either saturating ADP or limiting ATP concentrations, the enzyme binds 1 equivalent of Fe(III). F1ATPase pretreated with 5'-p- fluorosulfonylbenzoyladenosine, that selectively modifies the non-catalytic sites, binds only 1 mol of Fe(III)/mol of protein in the presence of either saturating ATP or ADP, Fe(III)-loaded F1ATPase containing either 1 or 2 equivalents of Fe(III) show identical EPR signals at g=4.3. The signals are not perturbed by the binding of nucleotides to the enzyme while they are altered by phosphate addition. These results indicate that F1ATPase contains two distinct Fe(III)-binding sites, which differ from nucleotide-binding sites, and that one of these sites is opened up for Fe(III) uptake by conformational changes induced by binding of ATP to the loose non-catalytic site.

References

Oct 10, 1979·Biochimica Et Biophysica Acta·F PeninD C Gautheron
Oct 15, 1992·The Biochemical Journal·V Zhelyaskov, K T Yue
Dec 16, 1991·Biochemical and Biophysical Research Communications·G LippeI Mavelli
Aug 25, 1994·Nature·R L Cross

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Citations

Mar 13, 2001·Biochemical and Biophysical Research Communications·S ContessiG Lippe
May 8, 2004·Biochemical Pharmacology·Stefania ContessiGiovanna Lippe
Sep 24, 1999·Biochemical and Biophysical Research Communications·F PolizioI Mavelli
Sep 25, 2002·Biochemical and Biophysical Research Communications·G LippeI Mavelli
Sep 18, 2007·Plant Physiology and Biochemistry : PPB·Adriana S RibeiroJulio A Mignaco

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