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Literature DB >> 3580491

Fluorescence and energy transfer of tryptophans in Aplysia myoglobin.

S M Janes, G Holtom, P Ascenzi, M Brunori, R M Hochstrasser.

Abstract

The fluorescence decay of tryptophan residues in apo and met Aplysia limacina myoglobin and sperm whale myoglobin were measured in aqueous solution at 10 degrees-15 degrees C. In all species, multiexponential behavior was observed in which the individual components displayed unique frequency-dependent emission characteristics. The results suggest that the tryptophan fluorescence in all met samples are quenched by rapid Forster energy transfer to the heme as predicted from the crystal geometry. Fluorescence from the apo protein is similar to that in solutions of free tryptophans. In addition, the fluorescence properties of the reversible thermal denaturation of Aplysia limacina met myoglobin was investigated between 25 degrees and 75 degrees C.

Entities: Chemical Species

Mesh：

Substances：
Myoglobin
Tryptophan

Year: 1987 PMID： 3580491 PMCID： PMC1329937 DOI： 10.1016/S0006-3495(87)83390-8

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

13 in total

8. Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin.

Authors: J Qin; G N La Mar
Journal: J Biomol NMR Date: 1992-11 Impact factor: 2.835

9. Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A (1)H-NMR and electronic absorbance study.

Authors: Daniela Delli Castelli; Elena Lovera; Paolo Ascenzi; Mauro Fasano
Journal: Protein Sci Date: 2002-09 Impact factor: 6.725

9 in total

Fluorescence and energy transfer of tryptophans in Aplysia myoglobin.

1. The kinetics of the recombination reaction between apomyoglobin and alkaline haematin.

2. The amino acid sequence of myoglobin from the mollusc Aplysia limacina.

3. Denaturation of Aplysia myoglobin. Equilibrium study.

4. Fluorescence studies of Aplysia and sperm whale apomyoglobins.

5. Subnanosecond motions of tryptophan residues in proteins.

6. Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale.

7. Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale.

8. Preparation and properties of apohemoglobin and reconstituted hemoglobins.

9. Equilibrium and kinetics of the reaction of Aplysia myoglobin with azide.

10. Time-resolved fluorescence and anisotropy decay of the tryptophan in adrenocorticotropin-(1-24).

1. Tryptophan-to-heme electron transfer in ferrous myoglobins.

2. Ligand-dependent conformational equilibria of serum albumin revealed by tryptophan fluorescence quenching.

3. Effect of disordered hemes on energy transfer rates between tryptophans and heme in myoglobin.

4. Molecular dynamics simulations of fluorescence polarization of tryptophans in myoglobin.

5. Tryptophan dynamics of the FK506 binding protein: time-resolved fluorescence and simulations.

6. Upconversion spectrophotofluorometry.

7. Origin of slow relaxation following photoexcitation of W7 in myoglobin and the dynamics of its hydration layer.

8. Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin.

9. Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A (1)H-NMR and electronic absorbance study.