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Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3.

作者信息

Richard P

机构信息

Département de Biologie Cellulaire et Moléculaire, CEA Saclay, Gif-sur-Yvette, France.

出版信息

Biochim Biophys Acta. 1996 Jul 31;1275(3):141-4. doi: 10.1016/0005-2728(96)00037-0.

DOI:10.1016/0005-2728(96)00037-0
PMID:8695629
Abstract

The F-type ATPase, TF0F1, from the thermophilic Bacillus PS3, which is free of nucleotides after isolation, was specifically loaded with one 2-azido ADP on a non-catalytic site. The enzyme was covalently modified to various extents and the rate of ATP synthesis and ATP hydrolysis was measured. Both ATP synthesis and ATP hydrolysis extrapolated to zero for covalently binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process.

摘要

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