NDLI: Redox-related conformational changes in Rhodobacter capsulatus cytochrome c2.

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Redox-related conformational changes in Rhodobacter capsulatus cytochrome c2.

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Redox-related conformational changes in Rhodobacter capsulatus cytochrome c2.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Cusanovich, M. A. Zhao, D. Hutton, H. M. Gooley, P. R. MacKenzie, N. E.
Description	Country affiliation: United States Author Affiliation: Zhao D ( Department of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson 85721, USA.)
Abstract	WEFT-NOESY and transfer WEFT-NOESY NMR spectra were used to determine the heme proton assignments for Rhodobacter capsulatus ferricytochrome c2. The Fermi contact and pseudo-contact contributions to the paramagnetic effect of the unpaired electron in the oxidized state were evaluated for the heme and ligand protons. The chemical shift assignments for the 1H and 15N NMR spectra were obtained by a combination of 1H-1H and 1H-15N two-dimensional NMR spectroscopy. The short-range nuclear Overhauser effect (NOE) data are consistent with the view that the secondary structure for the oxidized state of this protein closely approximates that of the reduced form, but with redox-related conformational changes between the two redox states. To understand the decrease in stability of the oxidized state of this cytochrome c2 compared to the reduced form, the structural difference between the two redox states were analyzed by the differences in the NOE intensities, pseudo-contact shifts and the hydrogen-deuterium exchange rates of the amide protons. We find that the major difference between redox states, although subtle, involve heme protein interactions, orientation of the heme ligands, differences in hydrogen bond networks and, possible alterations in the position of some internal water molecules. Thus, it appears that the general destabilization of cytochrome c2, which occurs on oxidation, is consistent with the alteration of hydrogen bonds that result in changes in the internal dynamics of the protein.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	9
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2000-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochrome c Group Chemistry Rhodobacter Capsulatus Enzymology Amino Acid Sequence Cytochromes C2 Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Oxidation-reduction Protein Conformation Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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