Proton nuclear magnetic resonance as a probe of differences in structure between the C102T and F82S,C102T variants of iso-1-cytochrome c from the yeast Saccharomyces cerevisiae

Differences in chemical shifts and in nuclear Overhauser effects between the C102T and F82S,C102T variants of Saccharomyces cerevisiae iso-1-cytochrome c in both the reduced and oxidized forms are reported and analyzed. There is evidence for small conformational differences in both oxidation states...

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Bibliographic Details
Published in:Biochemistry (Easton) 1991-07, Vol.30 (28), p.7033-7040
Main Authors: Gao, Yuan, Boyd, Jonathan, Pielak, Gary J, Williams, Robert J. P
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Biological and medical sciences
crystallography
cytochrome c
Cytochrome c Group - genetics
Cytochromes c
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Genetic Variation
Heme - genetics
Hemoproteins
iso-1-cytochrome c
Magnetic Resonance Spectroscopy
Metalloproteins
Molecular Sequence Data
N.M.R
nuclear magnetic resonance spectroscopy
nuclear Overhauser effect
Protein Conformation
Proteins
Protons
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
X-Ray Diffraction
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Summary:Differences in chemical shifts and in nuclear Overhauser effects between the C102T and F82S,C102T variants of Saccharomyces cerevisiae iso-1-cytochrome c in both the reduced and oxidized forms are reported and analyzed. There is evidence for small conformational differences in both oxidation states of the double variant near position 82. Differences in structure are more evident in the oxidized forms of the variants. These differences extend to distant parts of the protein. It is concluded that the oxidized double variant has undergone a small rearrangement of several regions of the protein that are linked by a hydrogen-bond network. It is shown that the rearrangement involves hydrogen bonds associated with the two heme propionates and associated water molecules. The deductions from nuclear magnetic resonance data are compared with the differences in the crystal structures of the reduced forms of wild-type protein and the F82S variant [Louie, G. V., Pielak, G. J., Smith, M., & Brayer, G. D. (1988) Biochemistry 27, 7870-7876].
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00242a032