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  Structural mapping of catalytic site with respect to alpha-subunit and noncatalytic site in yeast mitochondrial F1-ATPase using fluorescence resonance energy transfer.

Divita, G., Goody, R. S., Gautheron, D. C., & Di Pietro, A. (1993). Structural mapping of catalytic site with respect to alpha-subunit and noncatalytic site in yeast mitochondrial F1-ATPase using fluorescence resonance energy transfer. The Journal of Biological Chemistry, 268(18), 13178-13186.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-AA56-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-285A-0
Genre: Journal Article

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JBiolChem_268_1993_13178.pdf (Any fulltext), 2MB
 
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Divita, Gilles1, Author              
Goody, Roger S.1, Author              
Gautheron, Danielè C., Author
Di Pietro, Attilio, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The intrinsic tryptophan fluorescence of Schizosaccharomyces pombe mitochondrial F1 is a very sensitive probe to differentiate nucleotide binding to catalytic and noncatalytic sites (Divita, G., Di Pietro, A., Roux, B., and Gautheron, D. C. (1992) Biochemistry 31, 5791-5798), the catalytic site saturation producing quenching of Trp-257 fluorescence (Divita, G., Jault, J.-M., Gautheron, D. C., and Di Pietro, A. (1993) Biochemistry 32, 1017-1024). The present results indicate that two types of fluorescent nucleotide analogues, bearing either 2'(3')N-methylanthraniloyl (mant) or 2',3'-O-(2,4,6-trinitrophenyl) (TNP) group, exhibit high-affinity binding and behave similarly to the corresponding unmodified nucleotides. Selective binding of mant GDP to the catalytic site produces a marked quenching of intrinsic fluorescence which is due to resonance energy transfer between Trp-257 and the mant group. The high efficiency of the transfer allows the determination of a short distance, 10.5 A, indicating the close proximity of catalytic site and alpha-subunit Trp-257. Selective saturation of the noncatalytic site by TNP-ADP produces a marked quenching of the extrinsic fluorescence of mant GDP bound to the catalytic site, which is correlated to an important resonance energy transfer between the two fluorescent groups. A rather short distance of 17.5 A is calculated, indicating vicinity of catalytic and noncatalytic sites.

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Language(s): eng - English
 Dates: 1993-03-021992-12-291993-06-25
 Publication Status: Published in print
 Pages: 9
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 Rev. Method: Peer
 Identifiers: eDoc: 665100
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 268 (18) Sequence Number: - Start / End Page: 13178 - 13186 Identifier: ISSN: 0021-9258
CoNE: /journals/resource/954925410826_1