DOI: 10.1016/s0969-2126(98)00085-9. Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism

Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism

10.1016/s0969-2126(98)00085-9

Crossref journal-article

Elsevier BV

Structure (78)

Bibliography

Orriss, G. L., Leslie, A. G., Braig, K., & Walker, J. E. (1998). Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism. Structure, 6(7), 831â837.

Authors 4

George L Orriss (first)
Andrew GW Leslie (additional)
Kerstin Braig (additional)
John E Walker (additional)

References 36 Referenced 82

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10.1016/0022-2836(85)90313-4 / J. Mol. Biol / Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria by Walker (1985)
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10.1016/S0021-9258(17)39716-8 / J. Biol. Chem / Identification of the essential tyrosine residue in the β-subunit of bovine heart mitochondrial F1-ATPase that is modified by 7-chloro-4-nitro[14C]benzofurazan by Andrews (1984)
10.1111/j.1432-1033.1985.tb08875.x / Eur. J. Biochem / Tyrosine 311 of a β-chain is the essential residue specifically modified by 4-chloro-7-nitrobenzofurazan in bovine heart mitochondrial ATPase by Sutton (1985)
10.1021/bi00591a008 / Biochemistry / Reactivity of the β-subunit of Escherichia coli adenosine triphosphatase with 4-chloro-7-nitrobenzofurazan by Lunardi (1979)
10.1016/0003-9861(86)90184-0 / Arch. Biochem. Biophys / The use of dithionite to identify the essential tyrosine residue in the F1-ATPase from the thermophilic bacterium, PS3, that reacts with 7-chloro-4-nitrobenzofurazan by Verburg (1986)
10.1016/0003-9861(89)90234-8 / Arch. Biochem. Biophys / Selectivity of modification when latent and activated forms of the chloroplast F1-ATPase are inactivated by 7-chloro-4-nitrobenzofurazan by Ceccarelli (1989)
10.1016/0005-2728(74)90037-1 / Biochim. Biophys. Acta / Selective and reversible inhibition of the ATPase of Micrococcus denitrificans by 7-chloro-4-nitrobenzo-2-oxa-1,3 diazole by Ferguson (1974)
10.1016/0014-5793(70)80095-3 / FEBS Lett / The reactivity of SH groups with a fluorogenic reagent by Birkett (1970)
10.1016/0005-2795(74)90159-7 / Biochim. Biophys. Acta / A fluorescent probe for the coenzyme induced structural changes in glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle by Price (1974)
10.1111/j.1432-1033.1975.tb04121.x / Eur. J. Biochem / The mitochondrial ATPase. Selective modification of a nitrogen residue in the β-subunit by Ferguson (1975)
10.1016/S0021-9258(17)42609-3 / J. Biol. Chem / Identification of the lysine residue to which the 4-nitrobenzofurazan group migrates after the bovine mitochondrial F1-ATPase is inactivated with 7-chloro-4-nitro[14C]benzofurazan by Andrews (1984)
10.1016/0014-5793(85)80535-4 / FEBS Lett / Identification of the essential β-chain lysine residue from bovine heart mitochondrial ATPase specifically modified with nitrobenzofurazan by Sutton (1985)
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Dates

Type	When
Created	21 years, 2 months ago (June 8, 2004, 2:49 p.m.)
Deposited	4 years, 2 months ago (June 22, 2021, 9:10 p.m.)
Indexed	1 month, 3 weeks ago (June 27, 2025, 6:35 a.m.)
Issued	27 years, 1 month ago (July 1, 1998)
Published	27 years, 1 month ago (July 1, 1998)
Published Print	27 years, 1 month ago (July 1, 1998)

Funders 0

None

BibTeX

@article{Orriss_1998, title={Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism}, volume={6}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/s0969-2126(98)00085-9}, DOI={10.1016/s0969-2126(98)00085-9}, number={7}, journal={Structure}, publisher={Elsevier BV}, author={Orriss, George L and Leslie, Andrew GW and Braig, Kerstin and Walker, John E}, year={1998}, month=jul, pages={831–837} }

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