Abstract:
:High-affinity and cooperative binding of two Ca(2+) per ATPase (SERCA) occurs within the membrane-bound region of the enzyme. Direct measurements of binding at various Ca(2+) concentrations demonstrate that site-directed mutations within this region interfere selectively with Ca(2+) occupancy of either one or both binding sites and with the cooperative character of the binding isotherms. A transition associated with high affinity and cooperative binding of the second Ca(2+) and the engagement of N796 and E309 are both required to form a phosphoenzyme intermediate with ATP in the forward direction of the cycle and also to form ATP from phosphoenzyme intermediate and ADP in the reverse direction of the cycle. This transition, defined by equilibrium and kinetic characterization of the partial reactions of the enzyme cycle, extends from transmembrane helices to the catalytic site through a long-range linkage and is the mechanistic device for interconversion of binding and phosphorylation potentials.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Inesi G,Zhang Z,Lewis Ddoi
10.1016/S0006-3495(02)75247-8subject
Has Abstractpub_date
2002-11-01 00:00:00pages
2327-32issue
5eissn
0006-3495issn
1542-0086pii
S0006-3495(02)75247-8journal_volume
83pub_type
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