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

Peter Richard

doi:10.1016/0005-2728(96)00037-0

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

Peter Richard

Not published at VTT

Research output: Contribution to journal › Article › Scientific › peer-review

2 Citations (Scopus)

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	https://doi.org/10.1016/0005-2728(96)00037-0
Publication status	Published - 31 Jul 1996
MoE publication type	Not Eligible

Keywords

2-Azido nucleotide
Adenosine binding site
ATPase
ATPase TFF
F-type
H-
Thermophilic Bacillus PS3

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

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.",

keywords = "2-Azido nucleotide, Adenosine binding site, ATPase, ATPase TFF, F-type, H-, Thermophilic Bacillus PS3",

author = "Peter Richard",

year = "1996",

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doi = "10.1016/0005-2728(96)00037-0",

language = "English",

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AU - Richard, Peter

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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

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DO - 10.1016/0005-2728(96)00037-0

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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 -

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

Abstract

Keywords

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