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 covalentiy binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process.
| Original language | English |
|---|---|
| Pages (from-to) | 141-144 |
| Number of pages | 4 |
| Journal | Biochimica et Biophysica Acta: Bioenergetics |
| Volume | 1275 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 31 Jul 1996 |
| MoE publication type | Not Eligible |
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Keywords
- 2-Azido nucleotide
- Adenosine binding site
- ATPase
- ATPase TFF
- F-type
- H-
- Thermophilic Bacillus PS3
Cite this
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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. / Richard, Peter.
In: Biochimica et Biophysica Acta: Bioenergetics, Vol. 1275, No. 3, 31.07.1996, p. 141-144.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3
AU - Richard, Peter
PY - 1996/7/31
Y1 - 1996/7/31
N2 - 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 covalentiy binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process.
AB - 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 covalentiy binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process.
KW - 2-Azido nucleotide
KW - Adenosine binding site
KW - ATPase
KW - ATPase TFF
KW - F-type
KW - H-
KW - Thermophilic Bacillus PS3
UR - http://www.scopus.com/inward/record.url?scp=0030608150&partnerID=8YFLogxK
U2 - 10.1016/0005-2728(96)00037-0
DO - 10.1016/0005-2728(96)00037-0
M3 - Article
C2 - 8695629
AN - SCOPUS:0030608150
VL - 1275
SP - 141
EP - 144
JO - Biochimica et Biophysica Acta: Bioenergetics
JF - Biochimica et Biophysica Acta: Bioenergetics
SN - 0005-2728
IS - 3
ER -