A Differential Scanning Calorimetric Study of the Thermal Unfolding of Apo- and Holo-cytochrome B562

Overview

Journal Protein Sci

Specialty Biochemistry

Date 1998 May 6

PMID 9568902

Citations 7

Authors

C R Robinson

Y Liu

R OBrien

S G Sligar

J M STURTEVANT

Affiliations

Soon will be listed here.

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.

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