Abstract:
:Avidin, a basic tetrameric glycoprotein, isolated from hen egg-white, binds up to four molecules of biotin with exceptionally high affinity. The presence of tryptophanyl residues in the active site pointed out the opportunity of correlating the protein fluorescence with biotin binding. We have performed both steady state and dynamic fluorescence experiments using biotin or biotin-derived molecules (biotinamine, diaminobiotin and iminobiotin) as ligands. The fluorescence decay data can only be fitted by two continuous distributions of lifetimes which may reflect the presence of static or dynamic microheterogeneity in the environment of the tryptophan residues. We observed that the binding of biotin, biotinamine and iminobiotin reduces the widths of both distributions to discrete lifetimes thus indicating a more homogenous environment for the emitting tryptophan residues. Instead, the binding of diaminobiotin, which lacks the imidazolone ring, affects one lifetime distribution only. The binding of biotin also affects the rotational correlation time of avidin, which becomes shorter, suggesting a more compact structure of the ligated protein. The utility of analyzing the fluorescence in terms of distributions appears to be further warranted.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Mei G,Pugliese L,Rosato N,Toma L,Bolognesi M,Finazzi-Agrò Adoi
10.1006/jmbi.1994.1600subject
Has Abstractpub_date
1994-09-30 00:00:00pages
559-65issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(84)71600-7journal_volume
242pub_type
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