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Protein Science, Vol 7, Issue 4 961-965, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

A differential scanning calorimetric study of the thermal unfolding of apo- and holo-cytochrome b(562)

C. R. ROBINSON, Y. LIU, R. O'BRIEN, S. G. SLIGAR and J. M. STURTEVANT
Department of Biochemistry, University of Illinois, Champaign, Illinois 618001 Present address: 3-Dimensional Pharmaceuticals, 665 Stockton Drive, Exton, Pennsylvania 19341.

Cytochrome b(562) is a four-helix-bundle protein containing a non-covalently bound b-type heme prosthetic group. In the absence of heme, cytochrome b(562) 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 b(562) 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 b(562) is substantially destabilized relative to the holoprotein: the t(1/2) 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 b(562) denaturation are within the range of observed values for small proteins.
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