The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
How azide inhibits ATP hydrolysis by the F-ATPases
Open accessAbstract
In the structure of bovine F 1 -ATPase determined at 1.95-Å resolution with crystals grown in the presence of ADP, 5′-adenylyl-imidodiphosphate, and azide, the azide anion interacts with the β-phosphate of ADP and with residues in the ADP-binding catalytic subunit, β DP . It occupies a position between the catalytically essential amino acids, β-Lys-162 in the P loop and the “arginine finger” residue, α-Arg-373, similar to the site occupied by the γ-phosphate in the ATP-binding subunit, β TP . Its presence in the β DP -subunit tightens the binding of the side chains to the nucleotide, enhancing its affinity and thereby stabilizing the state with bound ADP. This mechanism of inhibition appears to be common to many other ATPases, including ABC transporters, SecA, and DNA topoisomerase IIα. It also explains the stimulatory effect of azide on ATP-sensitive potassium channels by enhancing the binding of ADP.
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Cites
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Oliver, D. B., Cabelli, R. J., Dolan, K. M., & Jarosik, G. P. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8227 · Cited by 311
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Gledhill, J. R., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706290104 · Cited by 379
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Gao, J., Li, J., Geng, W.-C., Chen, F.-Y., Duan, X., Zheng, Z., Ding, D., & Guo, D.-S. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b02331 · Cited by 266
Metadata
- Authors
- Bowler, M. W., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-06-06
- Volume
- 103
- Issue
- 23
- Pages
- 8646-8649
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2119010514
- Cited by
- 244
- References
- 2
- FWCI
- 4.05
- Type
- journal article
- Language
- en
- Open access
- green
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