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Electron microscopic observations of submitochondrial particles submitted to azide inhibition
Author(s) -
Valdivia Enrique,
Gabel Carol,
Spitsberg Vitaly,
Blondin George,
Garcia Jorge
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a295-d
Subject(s) - submitochondrial particle , azide , oxidative phosphorylation , chemistry , biophysics , electron transport chain , phosphorylation , mitochondrion , biochemistry , biology , organic chemistry
The objective of this study is to describe structural and biochemical alterations observed in submitochondrial particles submitted to azide inhibition which conserve oxidative phosphorylation. The azide inhibited particles demonstrate electron microscopic compact F1 headpieces, with oligomerization that may be required for ATP formation. Similar changes have been observed in isolated and crystallized ATP (F1) particles submitted to the presence of the F1 inhibitory protein. The molecular mechanism of azide inhibition has been demonstrated by Bowler et al. ( PNAS 103 :, 2006) as secondary to the binding of the anion azide to ADP in the D chain. These results suggest that oxidative phosphorylation require aggregation and solvent decrease of the F1 particles. (NIH and University of Wisconsin‐Madison Graduate School supported)