Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, NMR relaxation and deuterium exchange on the uniformly labeled protein-Reference-Cited by-同舟云学术

Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, NMR relaxation and deuterium exchange on the uniformly labeled protein

Published:2003-12 Issue:4-5 Volume:33 Page:193-201
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Cicero Daniel Oscar,Melino Sonia,Orsale Maria,Brancato Giuseppe,Amadei Andrea,Forlani Fabio,Pagani Silvia,Paci Maurizio

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference39 articles.

1. Westley J. Rhodanese and the sulfane pool. In: Jakoby WB, editor. The enzymatic basis of detoxification. New York: Academic Press; 1980. p. 245–61.

2. Characterization of a 12-Kilodalton Rhodanese Encoded by glpE of Escherichia coli and Its Interaction with Thioredoxin

3. Activation of porcine heart mitochondrial malate dehydrogenase by zero valence sulfur and rhodanese

4. Nitrogenase of Klebsiella pneumoniae. Rhodanese-catalysed restoration of activity of the inactive 2Fe species of the Fe protein

5. The covalent and tertiary structure of bovine liver rhodanese

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