The effects of exchange-inert metal-Nucleotide complexes on the kinetics of beef heart mitochondrial F1-ATPase

L. Steinke; R. Bacon; S. M. Schuster

doi:10.1016/0003-9861(87)90369-9

The effects of exchange-inert metal-Nucleotide complexes on the kinetics of beef heart mitochondrial F₁-ATPase

L. Steinke, R. Bacon, S. M. Schuster

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

3 Scopus citations

Abstract

The inhibition of beef heart mitochondrial F₁ by exchange-inert metal-nucleotide complexes was examined. Mono- and bidentate Cr(NH₃)₄ATP were found to be mixed noncompetitive inhibitors of F₁-catalyzed ATP hydrolysis (values of K_i = 0.5 and 0.1 mM; values of α = 0.2 and 24, respectively). Rh(H₂O)_nATP was also found to be a mixed noncompetitive inhibitor of F₁-catalyzed ATP hydrolysis (K_i = 0.3 mM, α = 0.7). These compounds were used in a series of dual inhibition experiments, along with mono- and bidentate CrATP and Co(NH₃)₄ATP. All the exchange-inert metal-nucleotides examined were found to be mutually exclusive inhibitors of F₁, indicating that they all bind to the same site(s). It is postulated that the pK_a of the metal-coordinated ligands is related to the potency of inhibition by these compounds. It appears probable that the exchangeinert nucleotide complexes are binding to site(s) in addition to the catalytic site(s) of F₁.

Original language	English (US)
Pages (from-to)	482-490
Number of pages	9
Journal	Archives of Biochemistry and Biophysics
Volume	258
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(87)90369-9
State	Published - Nov 1 1987

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

Access to Document

10.1016/0003-9861(87)90369-9

Cite this

@article{0c40120183c34b3d8e000cc9d088e37b,

title = "The effects of exchange-inert metal-Nucleotide complexes on the kinetics of beef heart mitochondrial F1-ATPase",

abstract = "The inhibition of beef heart mitochondrial F1 by exchange-inert metal-nucleotide complexes was examined. Mono- and bidentate Cr(NH3)4ATP were found to be mixed noncompetitive inhibitors of F1-catalyzed ATP hydrolysis (values of Ki = 0.5 and 0.1 mM; values of α = 0.2 and 24, respectively). Rh(H2O)nATP was also found to be a mixed noncompetitive inhibitor of F1-catalyzed ATP hydrolysis (Ki = 0.3 mM, α = 0.7). These compounds were used in a series of dual inhibition experiments, along with mono- and bidentate CrATP and Co(NH3)4ATP. All the exchange-inert metal-nucleotides examined were found to be mutually exclusive inhibitors of F1, indicating that they all bind to the same site(s). It is postulated that the pKa of the metal-coordinated ligands is related to the potency of inhibition by these compounds. It appears probable that the exchangeinert nucleotide complexes are binding to site(s) in addition to the catalytic site(s) of F1.",

author = "L. Steinke and R. Bacon and Schuster, {S. M.}",

note = "Funding Information: 1 This work was supported from the NSF. 2 Present address: Roche ology, Nutley, NJ 07110. 3 To whom correspondence",

year = "1987",

month = nov,

day = "1",

doi = "10.1016/0003-9861(87)90369-9",

language = "English (US)",

volume = "258",

pages = "482--490",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - The effects of exchange-inert metal-Nucleotide complexes on the kinetics of beef heart mitochondrial F1-ATPase

AU - Steinke, L.

AU - Bacon, R.

AU - Schuster, S. M.

N1 - Funding Information: 1 This work was supported from the NSF. 2 Present address: Roche ology, Nutley, NJ 07110. 3 To whom correspondence

PY - 1987/11/1

Y1 - 1987/11/1

N2 - The inhibition of beef heart mitochondrial F1 by exchange-inert metal-nucleotide complexes was examined. Mono- and bidentate Cr(NH3)4ATP were found to be mixed noncompetitive inhibitors of F1-catalyzed ATP hydrolysis (values of Ki = 0.5 and 0.1 mM; values of α = 0.2 and 24, respectively). Rh(H2O)nATP was also found to be a mixed noncompetitive inhibitor of F1-catalyzed ATP hydrolysis (Ki = 0.3 mM, α = 0.7). These compounds were used in a series of dual inhibition experiments, along with mono- and bidentate CrATP and Co(NH3)4ATP. All the exchange-inert metal-nucleotides examined were found to be mutually exclusive inhibitors of F1, indicating that they all bind to the same site(s). It is postulated that the pKa of the metal-coordinated ligands is related to the potency of inhibition by these compounds. It appears probable that the exchangeinert nucleotide complexes are binding to site(s) in addition to the catalytic site(s) of F1.

AB - The inhibition of beef heart mitochondrial F1 by exchange-inert metal-nucleotide complexes was examined. Mono- and bidentate Cr(NH3)4ATP were found to be mixed noncompetitive inhibitors of F1-catalyzed ATP hydrolysis (values of Ki = 0.5 and 0.1 mM; values of α = 0.2 and 24, respectively). Rh(H2O)nATP was also found to be a mixed noncompetitive inhibitor of F1-catalyzed ATP hydrolysis (Ki = 0.3 mM, α = 0.7). These compounds were used in a series of dual inhibition experiments, along with mono- and bidentate CrATP and Co(NH3)4ATP. All the exchange-inert metal-nucleotides examined were found to be mutually exclusive inhibitors of F1, indicating that they all bind to the same site(s). It is postulated that the pKa of the metal-coordinated ligands is related to the potency of inhibition by these compounds. It appears probable that the exchangeinert nucleotide complexes are binding to site(s) in addition to the catalytic site(s) of F1.

UR - http://www.scopus.com/inward/record.url?scp=0023442647&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023442647&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(87)90369-9

DO - 10.1016/0003-9861(87)90369-9

M3 - Article

C2 - 2890328

AN - SCOPUS:0023442647

SN - 0003-9861

VL - 258

SP - 482

EP - 490

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 2

ER -

The effects of exchange-inert metal-Nucleotide complexes on the kinetics of beef heart mitochondrial F₁-ATPase

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this