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Inhibitory Mg-ADP-fluoroaluminate complexes bound to catalytic sites of F(1)-ATPases: are they ground-state or transition-state analogs?

Autor: W S, Allison, H, Ren, C, Dou

Publikováno v: Journal of bioenergetics and biomembranes. 32(5)

Schemes are proposed for coupling sequential opening and closing the three catalytic sites of F(1) to rotation of the gamma subunit during ATP synthesis and hydrolysis catalyzed by the F(o)F(1)-ATP synthase. A prominent feature of the proposed mechan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f095913a266ffd6fc0bf1902c212edc2
https://pubmed.ncbi.nlm.nih.gov/15254389

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The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP

Autor: C, Dou, P A, Fortes, W S, Allison

Publikováno v: Biochemistry. 37(47)

The hydrolytic properties of the alpha3beta3gamma and mutant alpha3(betaY341W)3gamma subcomplexes of the TF1-ATPase have been compared. ATPase activity of the mutant is less sensitive to turnover-dependent inhibition by azide, less suppressed by incr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8fb39bfe16a26c8a353550c2e0ffb623
https://pubmed.ncbi.nlm.nih.gov/9843446

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ADP-fluoroaluminate complexes are formed cooperatively at two catalytic sites of wild-type and mutant alpha3beta3gamma subcomplexes of the F1-ATPase from the thermophilic Bacillus PS3

Autor: C, Dou, N B, Grodsky, T, Matsui, M, Yoshida, W S, Allison

Publikováno v: Biochemistry. 36(12)

Addition of Al3+ and F- to the alpha3beta3gamma subcomplex of the TF1-ATPase containing MgADP in one catalytic site causes slow, complete inactivation as the ADP-fluoroaluminate complex is formed. This conflicts with the "bisite" stochastic model sug

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::817f10a26a21a21ee5925a61c5d3412b
https://pubmed.ncbi.nlm.nih.gov/9132025

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Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP

Autor: J M, Jault, W S, Allison

Publikováno v: The Journal of biological chemistry. 269(1)

Prior incubation of the bovine heart mitochondrial F1-ATPase depleted of endogenous nucleotides (nd-MF1) with saturating ADP in the presence or absence of Mg2+ induces inhibition of hydrolysis of 2 mM ATP or ITP. After incubation of nd-MF1 with free

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e8ddbd6bcf7a34a315e8983597ea0720
https://pubmed.ncbi.nlm.nih.gov/8276813

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The TF1-ATPase and ATPase activities of assembled alpha 3 beta 3 gamma, alpha 3 beta 3 gamma delta, and alpha 3 beta 3 gamma epsilon complexes are stimulated by low and inhibited by high concentrations of rhodamine 6G whereas the dye only inhibits the alpha 3 beta 3, and alpha 3 beta 3 delta complexes

Autor: S R, Paik, K, Yokoyama, M, Yoshida, T, Ohta, Y, Kagawa, W S, Allison

Publikováno v: Journal of bioenergetics and biomembranes. 25(6)

The ATPase activity of the F1-ATPase from the thermophilic bacterium PS3 is stimulated at concentrations of rhodamine 6G up to about 10 microM where 70% stimulation is observed at 36 degrees C. Half maximal stimulation is observed at about 3 microM d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bc9cb39f3de9a103d06aa0dfaa7ada14
https://pubmed.ncbi.nlm.nih.gov/8144495

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Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase

Autor: J M, Jault, W S, Allison

Publikováno v: The Journal of biological chemistry. 268(3)

The bovine heart mitochondrial F1-ATPase depleted of nucleotides (nd-MF1) hydrolyzes 50 microM ATP in three kinetic phases at 30 degrees C. An initial "burst" rapidly transforms into an intermediate, slower rate, which slowly accelerates to the final

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0b42ff0735c4f9167acc0bd65bb06cb3
https://pubmed.ncbi.nlm.nih.gov/8420930

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Irradiation of the bovine mitochondrial F1-ATPase previously inactivated with 5'-p-fluorosulfonylbenzoyl-8-azido-[3H]adenosine cross-links His-beta 427 to Tyr-beta 345 within the same beta subunit

Autor: S, Zhuo, S, Garrod, P, Miller, W S, Allison

Publikováno v: The Journal of biological chemistry. 267(18)

The bovine heart mitochondrial F1-ATPase (MF1) is inactivated by 5'-p'-fluorosulfonylbenzoyl-8-azidoadenosine (8-N3-FSBA) with an apparent Kd of 0.47 mM at pH 8.0 and 23 degrees C in the absence of light. Irradiation of dark-inactivated enzyme with l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7262f16fb14bd2147ec2c1f8a8a017d7
https://pubmed.ncbi.nlm.nih.gov/1320008

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Tyrosine alpha 244 is derivatized when the bovine heart mitochondrial F1-ATPase is inactivated with 5'-p-fluorosulfonylbenzoylethenoadenosine

Autor: J G, Verburg, W S, Allison

Publikováno v: The Journal of biological chemistry. 265(14)

The bovine heart mitochondrial F1-ATPase (MF1) is inactivated by 5'-p-fluorosulfonylbenzoylethenoadenosine (FSB epsilon A) with pseudo-first order kinetics. The dependence of the rate of inactivation on the concentration of FSB epsilon A revealed an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::af6932f3ba5ad3d72c547c7d22611371
https://pubmed.ncbi.nlm.nih.gov/2139876

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