Biochimica et Biophysica Acta (BBA) - Protein Structure
Volume 669, Issue 1, 29 June 1981, Pages 13-20
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c
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Cited by (16)
Humanlike substitutions to Ω-loop D of yeast iso-1-cytochrome c only modestly affect dynamics and peroxidase activity
2018, Journal of Inorganic BiochemistryCitation Excerpt :It also grew in abruptly above pH 9.5 with an apparent pKa of 10.75 and n ~ 4. High pH fast phases on the 10–50 ms time scale for the alkaline transition have been reported previously for mammalian cytochromes c [49–53]. These phases have been attributed to unfolding of the least stable substructure of Cytc [49], formation of a weakened heme-Met80 bond [51,52] or displacement of Met80 by hydroxide [51].
Folding units govern the cytochrome c alkaline transition
2003, Journal of Molecular BiologyThe reaction of cytochrome c from different species with cytochrome c oxidase immobilized in an electrode supported lipid bilayer membrane
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1993, Journal of Electroanalytical ChemistryResonance raman spectroscopic characterization of the heme coordination and spin state in the alkaline form of horseradis peroxidase
1984, Biochimica et Biophysica Acta (BBA)/Protein Structure and MolecularNaturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity
2019, Journal of Physical Chemistry B
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