Effects of Fe(III) binding to the nucleotide‐independent site of F1‐ATPase: enzyme thermostability and response to activating anions

FEBS Letters

Lippe, Giovanna²  Scirè, Andrea¹  Mavelli, Irene²  Contessi, Stefania²  Tanfani, Fabio¹ 

[1] Istituto di Biochimica, Facoltà di Medicina e Chirurgia, Università di Ancona, via Ranieri, 60131 Ancona, Italy;Dipartimento di Scienze e Tecnologie Biomediche, Università di Udine, p.le Kolbe 4, 33100 Udine, Italy

关键词: F1-ATPase;    Fe(III) binding site;    Fourier transform infrared spectroscopy;    Anion activation;    FT-IR;    Fourier transform infrared spectroscopy;    AMP-PNP;    β;    γ-imidoadenosine 5′-triphosphate;   

DOI  :  10.1016/S0014-5793(01)02908-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mitochondrial F₁-ATPase was induced in different conformations by binding of specific ligands, such as nucleotides. Then, Fourier transform infrared spectroscopy (FT-IR) and kinetic analyses were run to evaluate the structural and functional effects of Fe(III) binding to the nucleotide-independent site. Binding of one equivalent of Fe(III) induced a localised stabilising effect on the F₁-ATPase structure destabilised by a high concentration of NaCl, through rearrangements of the ionic network essential for the maintenance of enzyme tertiary and/or quaternary structure. Concomitantly, a lower response of ATPase activity to activating anions was observed. Both FT-IR and kinetic data were in accordance with the hypothesis of the Fe(III) site location near one of the catalytic sites, i.e. at the α/β subunit interface.

【 授权许可】

Unknown