Tryptophan Phosphorescence Spectroscopy Reveals That a Domain in the NAD(H)-binding Component (dI) of Transhydrogenase from Rhodospirillum rubrum Has an Extremely Rigid and Conformationally Homogeneous Protein Core-Reference-Cited by-同舟云学术

Tryptophan Phosphorescence Spectroscopy Reveals That a Domain in the NAD(H)-binding Component (dI) of Transhydrogenase from Rhodospirillum rubrum Has an Extremely Rigid and Conformationally Homogeneous Protein Core

Published:2003-11 Issue:48 Volume:278 Page:47578-47584
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Broos Jaap,Gabellieri Edi,van Boxel Gijs I.,Jackson J. Baz,Strambini Giovanni B.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. The Alternating Site, Binding Change Mechanism for Proton Translocation by Transhydrogenase

2. Protein–protein recognition, hydride transfer and proton pumping in the transhydrogenase complex11Because Structure with Folding & Design operates a ‘Continuous Publication System’ for Research Papers, this paper has been published on the internet before being printed (accessed from http://biomednet.com/cbiology/str). For further information, see the explanation on the contents page.

3. Crystal Structures of Transhydrogenase Domain I with and without Bound NADH,

4. The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria

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