A comparative picosecond-resolved fluorescence study of tryptophan residues in iron-sulfur proteins-Reference-Cited by-同舟云学术

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A comparative picosecond-resolved fluorescence study of tryptophan residues in iron-sulfur proteins

Published:1994-07-18 Issue:3 Volume:348 Page:305-310
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Dorovska-Taran Victoria,van Hoek Arie,Link Thomas A.,Visser Antonie J.W.G.,Hagen Wilfred R.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)00606-7/fullpdf

Reference27 articles.

1. Ferredoxin from Halobacterium of the Dead Sea. Structural properties revealed by fluorescence techniques

2. pH-induced conformational changes in spinach ferredoxin: Steady-state and time-resolved fluorescence studies

3. Nature of the Non-Haem Iron in Ferredoxin and Rubredoxin

4. [39] Ferredoxins from photosynthetic bacteria, algae, and higher plants

5. Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster

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1. Red-Ox Reactions with NADH Dehydrogenase;Biophysics of Mitochondria;2019

2. Solar cells based on the poly(N-vinylcarbazole): porphyrin: tris(8-hydroxyquinolinato) aluminium blend system*;Chinese Physics B;2011-03-01

3. Studies on the degradation pathway of iron-sulfur centers during unfolding of a hyperstable ferredoxin: cluster dissociation, iron release and protein stability;JBIC Journal of Biological Inorganic Chemistry;2004-10-02

4. Release of Flavin Adenine Dinucleotide in the Course of a Local Conformational Transition Induced by Trimethylamine Dehydrogenase in Electron-Transferring Flavoprotein;Russian Journal of Bioorganic Chemistry;2004-05

5. Femtosecond dynamics of rubredoxin: Tryptophan solvation and resonance energy transfer in the protein;Proceedings of the National Academy of Sciences;2001-12-18

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