Beef-heart mitochondrial F1-ATPase can use endogenous bound phosphate to synthesize ATP in dimethyl sulfoxide
نویسندگان
چکیده
منابع مشابه
The unbinding of ATP from F1-ATPase.
Using molecular dynamics, we study the unbinding of ATP in F(1)-ATPase from its tight binding state to its weak binding state. The calculations are made feasible through use of interpolated atomic structures from Wang and Oster [Nature 1998, 396: 279-282]. These structures are applied to atoms distant from the catalytic site. The forces from these distant atoms gradually drive a large primary r...
متن کاملTightly bound magnesium in mitochondrial adenosine triphosphatase from beef heart.
Tightly bound magnesium was found in soluble, purified ATPase (F1) from beef heart mitochondria in the amount of 1 mol/mol of F1. Iron, zinc, cobalt, manganese, calcium, sodium, copper, and potassium were not tightly bound at stoichiometric levels. Removal of magnesium by chelating agents caused loss of ATPase activity. Removal of tightly bound nucleotide by gel filtration in 50% glycerol- or 6...
متن کاملTightly Bound Magnesium in Mitochondrial Adenosine Triphosphatase from Beef Heart*
Tightly bound magnesium was found in soluble, purified ATPase (F,) from beef heart mitochondria in the amount of 1 mol/mol of F1. Iron, zinc, cobalt, manganese, calcium, sodium, copper, and potassium were not tightly bound at stoichiometric levels. Removal of magnesium by chelating agents caused loss of ATPase activity. Removal of tightly bound nucleotide by gel filtration in 50% glycerolor 60 ...
متن کاملATP hydrolysis assists phosphate release and promotes reaction ordering in F1-ATPase
F1-ATPase (F1) is a rotary motor protein that can efficiently convert chemical energy to mechanical work of rotation via fine coordination of its conformational motions and reaction sequences. Compared with reactant binding and product release, the ATP hydrolysis has relatively little contributions to the torque and chemical energy generation. To scrutinize possible roles of ATP hydrolysis, we ...
متن کاملNucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.
We have studied the properties of beef heart mitochondrial F1 having inhibitory MgADP bound at one of the three catalytic sites and various levels of occupancy of the three noncatalytic nucleotide sites including zero, two, or three ADP/ATPs or two ADP/ATP plus one GTP. The properties examined include the rate of MgATP-dependent reactivation and the rate of increase in the fraction of F1 contai...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1991
ISSN: 0014-5793
DOI: 10.1016/0014-5793(91)81302-o