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Literature summary for 1.11.1.5 extracted from

  • Sterckx, Y.G.; Volkov, A.N.
    Cofactor-dependent structural and binding properties of yeast cytochrome C peroxidase (2014), Biochemistry, 53, 4526-4536 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
apo and holo CcP exhibit very similar structural, hydrodynamic, and thermodynamic properties. Apo CcP is more expanded in solution, displays a number of characteristics associated with a molten globule state, and does not form an unfolding intermediate during thermal and chemical denaturation Saccharomyces cerevisiae

General Stability

General Stability Organism
in presence of guanidinium HCl, both apo and holo CcP exhibit single transitions, with midpoints of 1.34 M and 1.40 M for apo and holo CcP, rrespectively Saccharomyces cerevisiae
in presence of urea, the transition midpoint is 4.12 M for apo CcP and 3.72 M for the holo protein Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
56.1
-
melting temperature, apo CcP Saccharomyces cerevisiae
58
-
melting temperature, holo CcP Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
cytochrome c holo CcP binds cytochrome c with micromolar affinity. For apo CcP, the interaction with cytochrome c is completely abolished Saccharomyces cerevisiae