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• W2075060166 abstract "Cytochrome b562 is a four-helix-bundle protein containing a non-covalently bound b-type heme prosthetic group. In the absence of heme, cytochrome b562 remains highly structured under native conditions. Here we report thermodynamic data for the thermal denaturation of the holo- and apoproteins as determined by differential scanning calorimetry. Thermal denaturation of holocytochrome b562 is a highly reversible process, and unexpectedly does not involve dissociation of the heme prosthetic group. Thermal denaturation of the corresponding apoprotein, with the heme group chemically removed, remains a cooperative, reversible process. Apocytochrome b562 is substantially destabilized relative to the holoprotein: the t1/2 is more than ten degrees lower, and enthalpy and heat capacity changes are about one-half of the holoprotein values. However, the energetic parameters of apocytochrome b562 denaturation are within the range of observed values for small proteins." @default.
• W2075060166 created "2016-06-24" @default.
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• W2075060166 date "1998-04-01" @default.
• W2075060166 modified "2023-10-16" @default.
• W2075060166 title "A differential scanning calorimetric study of the thermal unfolding of apo- and holo-cytochrome<i>b</i>₅₆₂" @default.
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• W2075060166 doi "https://doi.org/10.1002/pro.5560070413" @default.
• W2075060166 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2143982" @default.
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• W2075060166 hasPublicationYear "1998" @default.
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