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Author (up) Bayley, P.; Martin, S.; Anson, M.
Title Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution Type Journal Article
Year 1975 Publication Biochemical and Biophysical Research Communications Abbreviated Journal Biochem Biophys Res Commun
Volume 66 Issue 1 Pages 303-308
Keywords *Alcohol Oxidoreductases/metabolism; Animals; Circular Dichroism; Horses; Kinetics; Liver/enzymology; Mathematics; Protein Conformation; Temperature; Time Factors
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Language English Summary Language Original Title
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ISSN 0006-291X ISBN Medium
Area Expedition Conference
Notes PMID:1172440 Approved no
Call Number Equine Behaviour @ team @ Serial 3816
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Author (up) Hirota, S.; Suzuki, M.; Watanabe, Y.
Title Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c Type Journal Article
Year 2004 Publication Biochemical and Biophysical Research Communications Abbreviated Journal Biochem Biophys Res Commun
Volume 314 Issue 2 Pages 452-458
Keywords Amino Acids/chemistry; Animals; Cytochromes c/*chemistry; Heme/*chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium/chemistry; Peptides/chemistry; Protein Folding; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine/*analogs & derivatives/*chemistry
Abstract Effect of a hydrophobic peptide on folding of oxidized cytochrome c (cyt c) is studied with trityrosine. Folding of cyt c was initiated by pH jump from 2.3 (acid-unfolded) to 4.2 (folded). The Soret band of the 2-ms transient absorption spectrum during folding decreased its intensity and red-shifted from 397 to 400 nm by interaction with trityrosine, whereas tyrosinol caused no significant effect. The change in the transient absorption spectrum by interaction with trityrosine was similar to that obtained with 100 mM imidazole, which showed that the population of the intermediate His/His coordinated species increased during folding of cyt c by interaction with trityrosine. The absorption change was biphasic, the fast phase (82+/-9s(-1)) corresponding to the transition from the His/H(2)O to the His/Met coordinated species, whereas the slow phase (24+/-3s(-1)) from His/His to His/Met. By addition of trityrosine, the relative ratio of the slow phase increased, due to increase of the His/His species at the initial stage of folding. According to the resonance Raman spectra of cyt c, the high-spin 6-coordinate and low-spin 6-coordinate species were dominated at pH 2.3 and 4.2, respectively, and these species were not affected by addition of trityrosine. These results demonstrated that the His/His species increased by interaction with trityrosine at the initial stage of cyt c folding, whereas the heme coordination structure was not affected by trityrosine when the protein was completely unfolded or folded. Hydrophobic peptides thus may be useful to study the effects of hydrophobic interactions on protein folding.
Address Department of Physical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, 607-8414 Kyoto, Japan. hirota@mb.kyoto-phu.ac.jp
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ISSN 0006-291X ISBN Medium
Area Expedition Conference
Notes PMID:14733927 Approved no
Call Number Equine Behaviour @ team @ Serial 3777
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Author (up) Jallon, J.M.; Risler, Y.; Iwatsubo, M.
Title Beef liver L-Glutamate dehydrogenase mechanism: presteady state study of the catalytic reduction of 2.oxoglutarate by NADPH Type Journal Article
Year 1975 Publication Biochemical and biophysical research communications Abbreviated Journal Biochem Biophys Res Commun
Volume 67 Issue 4 Pages 1527-1536
Keywords Animals; Cattle; Glutamate Dehydrogenase/*metabolism; Ketoglutaric Acids; Kinetics; Liver/*enzymology; Nadp; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet
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Language English Summary Language Original Title
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ISSN 0006-291X ISBN Medium
Area Expedition Conference
Notes PMID:1038 Approved no
Call Number Admin @ knut @ Serial 21
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