Výsledky vyhledávání - "Y M, Milgrom"

Nucleotide-binding sites on Escherichia coli F1-ATPase. Specificity of noncatalytic sites and inhibition at catalytic sites by MgADP

Autor: Y M Milgrom, E A Bramhall, Richard L. Cross, D J Hyndman

Publikováno v: Journal of Biological Chemistry. 269:28871-28877

Nucleotide-depleted EcF1 binds a maximum of two GTP, ATP, or ADP at noncatalytic sites, whereas all three sites can only be filled by a combination of nucleoside di- and triphosphates. MgPPi prevents binding of GTP and significantly slows ATP binding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::50a042400864717a23137bea79164a9b
https://doi.org/10.1016/s0021-9258(19)61988-5

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Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites

Autor: Y M Milgrom, Richard L. Cross

Publikováno v: Journal of Biological Chemistry. 268:23179-23185

We have studied the properties of beef heart mitochondrial F1 having inhibitory MgADP bound at one of the three catalytic sites and various levels of occupancy of the three noncatalytic nucleotide sites including zero, two, or three ADP/ATPs or two A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::15943cbda79292ed77b9ec11d36441d7
https://doi.org/10.1016/s0021-9258(19)49444-1

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Probes of inhibition of Escherichia coli F(1)-ATPase by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole in the presence of MgADP and MgATP support a bi-site mechanism of ATP hydrolysis by the enzyme

Autor: Y. M. Milgrom, V. V. Bulygin

Publikováno v: Biochemistry. Biokhimiia. 75(3)

Binding of MgADP and MgATP to Escherichia coli F(1)-ATPase (EcF(1)) has been assessed by their effects on extent of the enzyme inhibition by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole (NBD-Cl). MgADP at low concentrations (K(d) 1.3 microM) promotes the i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cffb4a4dd10fdbf379f6268fac33994
https://pubmed.ncbi.nlm.nih.gov/20370611

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The permeability transition in heart mitochondria is regulated synergistically by ADP and cyclosporin A

Autor: Y M Milgrom, Gerald P. Brierley, Sergei A. Novgorodov, Tatyana I. Gudz

Publikováno v: Journal of Biological Chemistry. 267:16274-16282

Heart mitochondria respiring in a sucrose medium containing P(i) show a permeability transition when challenged with Ca2+ and an oxidant such as cumene hydroperoxide. The transition results from the opening of a Ca(2+)-dependent pore and is evidenced

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::171d298347ac7823eec4d9fd35838f36
https://doi.org/10.1016/s0021-9258(18)41996-5

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The characteristics and effect on catalysis of nucleotide binding to noncatalytic sites of chloroplast F1-ATPase

Autor: Y M Milgrom, L L Ehler, Paul D. Boyer

Publikováno v: Journal of Biological Chemistry. 266:11551-11558

The recent finding that the presence of ATP at non-catalytic sites of chloroplast F1-ATPase (CF1) is necessary for ATPase activity (Milgrom, Y. M., Ehler, L. L., and Boyer, P. D. (1990) J. Biol. Chem. 265,18725-18728) prompted more detailed studies o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b765842466c4d214d1aafa1c59845ebe
https://doi.org/10.1016/s0021-9258(18)98992-1

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ATP binding at noncatalytic sites of soluble chloroplast F1-ATPase is required for expression of the enzyme activity

Autor: L L Ehler, Y M Milgrom, Paul D. Boyer

Publikováno v: Journal of Biological Chemistry. 265:18725-18728

The F1-ATPase from chloroplasts (CF1) lacks catalytic capacity for ATP hydrolysis if ATP is not bound at noncatalytic sites. CF1 heat activated in the presence of ADP, with less than one ADP and no ATP at non-catalytic sites, shows a pronounced lag i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8a96a5fb13e55714fa9781dadb4671bb
https://doi.org/10.1016/s0021-9258(17)30568-9

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Studies on reconstitution of the Rhodospirillum rubrum nicotinamide nucleotide transhydrogenase

Autor: Y M, Milgrom, Y, Hatefi

Publikováno v: Biochemistry and molecular biology international. 34(6)

The energy-transducing nicotinamide nucleotide transhydrogenase of Rhodospirillum rubrum is composed of 3 subunits alpha 1, alpha 2 and beta, with M(r) values, respectively, of 40.3, 14.9 and 47.8 kDa. Subunit alpha 1 is water-soluble, loosely bound

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9d1d415cfd4d04030f50c66d9efd7c01
https://pubmed.ncbi.nlm.nih.gov/7696982

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