Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase.

Literature DB >> 158596

Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase.

Abstract

ATP concentration modulates oxygen exchange catalyzed by purified, soluble mitochondrial ATPase during ATP hydrolysis so that water oxygen incorporation into each Pi formed increases markedly as ATP concentration is lowered. This behavior is readily explained by catalytic cooperativity between subunits of the ATPase. However, other reasonable explanations also need consideration. A new approach for assessing these various explanations is used, based on measurement of the [18O]Pi species formed by hydrolysis of ATP highly labeled with 18O in the gamma-phosphoryl group. The results and other supporting data give what appears to be the most compelling evidence yet attained for alternating site catalytic cooperativity in an enzymic catalysis.

Entities: Chemical Gene

Mesh：

Substances：

Year: 1979 PMID： 158596

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

Keyword Cloud
Cited

18 in total

1. Cooperativity between the enzymatic sites of F1-ATPase revisited by the use of HPLC methods.

Authors: G Berger; G Girault; J L Zimmermann
Journal: J Bioenerg Biomembr Date: 1998-12 Impact factor: 2.945

Review 2. Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1.

Authors: R L Cross; T M Duncan
Journal: J Bioenerg Biomembr Date: 1996-10 Impact factor: 2.945

3. Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme.

Authors: V N Kasho; P D Boyer
Journal: Proc Natl Acad Sci U S A Date: 1989-11 Impact factor: 11.205

Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase.

1. Cooperativity between the enzymatic sites of F1-ATPase revisited by the use of HPLC methods.

Review 2. Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1.

3. Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme.

4. High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase.

5. Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis.

Review 6. Chemical modification of active sites in relation to the catalytic mechanism of F1.

Review 7. Mechanism of F1-ATPase studied by the genetic approach.

Review 8. Molecular genetics of F1-ATPase from Escherichia coli.

Review 9. The proton-ATPase of bacteria and mitochondria.

Review 10. Recent developments on structural and functional aspects of the F1 sector of H+-linked ATPases.