Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi.

  title={Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi.},
  author={Tadeusz Kulinski and Antonie J.W.G. Visser and Dennis J. O'Kane and J Lee},
  volume={26 2},
Spectroscopic techniques have been applied to investigate the conformation, local structure, and dynamic properties of the apoprotein of the lumazine protein from Photobacterium leiognathi and the holoprotein reconstituted with either the natural ligand 6,7-dimethyl-8-ribityllumazine or the closely related analogues riboflavin and 6-methyl-7-oxo-8-ribityllumazine (7-oxolumazine). The analogues are bound similarly to the natural prosthetic group. They exhibit similar shifts on binding in their… 
Fluorescence study of the ligand stereospecificity for binding to lumazine protein.
The influence of the stereoconfiguration at the 8-position found for lumazine protein parallels that previously observed for the enzyme riboflavin synthase, where the lumazines are substrates or inhibitors.
Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates.
Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with theLuciferase hydroxyflavin fluorescent transient and the Luciferase peroxyflavin intermediates.
Time-resolved fluorescence studies of flavodoxin. Fluorescence decay and fluorescence anisotropy decay of tryptophan in Desulfovibrio flavodoxins
By comparing the results of protein preparations of normal and FMN-depleted flavodoxin, radiationless energy transfer from tryptophan to FMN has been demonstrated, and the anisotropy decay of both Desulfovibrio FMn-depicted flavodoxins is exponential, whereas that of the two holoproteins is clearly non-exponential.
Flavin dynamics in reduced flavodoxins. A time-resolved polarized fluorescence study.
Fluorescence anisotropy decays show that the flavin mononucleotide in all four reduced flavodoxins is immobilized within the protein matrix, as indicated by the recovery of a single rotational correlation time, reflecting the rotation of the whole protein.
Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1.
It is shown that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine-bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi.
Tryptophan-BODIPY: a versatile donor-acceptor pair for probing generic changes of intraprotein distances.
We demonstrate that Tryptophan (Trp) and N-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-yl)methyl iodoacetamide (BODIPY) is a suitable donor-acceptor (D-A) pair for intraprotein
Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosum.
The stability of the vanadium containing bromoperoxidase from Ascophyllum nodosum was studied and the data suggest that the protonation of a group with a pKa higher than 8.5 prevents the binding of vanadate.
Interaction of the fluorescent probe RH421 with ribulose-1,5-bisphosphate carboxylase/oxygenase and with Na+,K(+)-ATPase membrane fragments.
The fluorescent response of RH421 to the ATP-induced conformational change of the Na+,K+-ATPase is consistent with either a redistribution of dye from the liquid-crystalline lipid matrix into the vicinity of membrane protein or a reorganisation of the lipids surrounding the protein into a more rigid structure caused by the conformational changes of the protein.
Time-resolved fluorescence spectroscopy of lumazine protein from Photobacterium phosphoreum using synchrotron radiation
It was found that the tryptophan residue has a large motional freedom as also reported previously for this protein and for the related protein from P. leiognathi.
Changes in secondary structure and flavin microenvironment between Azotobacter vinelandii lipoamide dehydrogenase and several deletion mutants from circular dichroism
Circular dichroism (CD) has been used to investigate the secondary structure of wild-type lipoamide dehydrogenase from Azotobacter vinelandii and two deletion mutants lacking 9 and 14 C-terminal