Effect of inhibitor binding to β subunits of F1ATPase on enzyme thermostability: a kinetic and FT-IR spectroscopic analysis-Reference-Cited by-同舟云学术

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Effect of inhibitor binding to β subunits of F1ATPase on enzyme thermostability: a kinetic and FT-IR spectroscopic analysis

Published:1998-08-07 Issue:3 Volume:432 Page:128-132
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Lippe Giovanna,Tanfani Fabio,Di Pancrazio Francesca,Contessi Stefania,Bertoli Enrico,Dabbeni-Sala Federica

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(98)00816-3/fullpdf

Reference20 articles.

1. Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine.

2. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

3. Adenine nucleotide binding sites on beef heart F1-ATPase. Asymmetry and subunit location.

4. Adenine nucleotide-binding sites on beef heart F1-ATPase. Conditions that affect occupancy of catalytic and noncatalytic sites.

5. The binding change mechanism for ATP synthase — Some probabilities and possibilities

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Effects of Fe(III) binding to the nucleotide-independent site of F1-ATPase: enzyme thermostability and response to activating anions;FEBS Letters;2001-09-26

2. Isolation and characterization of mitochondrial F1-ATPase from crayfish (Orconectes virilis) gills;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2001-02

3. Thermal denaturation pathway of starch phosphorylase fromCorynebacterium callunae: Oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the protein;Protein Science;2000

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