Abstract：
:Oxidized cytochrome c oxidase exists in two reasonably well-defined conformations, a high-spin conformation with maximal absorption at 418 nm and a low-spin conformation with maximal absorption at 428 nm. The equilibrium between these two conformations has been studied as a function of pH, pressure, and temperature. pH effects the equilibrium between the two conformations, the maximum fraction of the 418-nm form being found at about pH 6.8. Increasing pressure displaced the equilibrium toward the 428-nm form; the molar volume changes found are independent of pH but strongly dependent on temperature. Increasing temperature over the range -20 to 25 degrees C displaces the equilibrium toward the 428-nm form; the van't Hoff plots that result show a discontinuity at about 10 degrees C. Above 10 degrees C, delta H is relatively constant as a function of pH; below 10 degrees C, delta H is strongly pH dependent. Delta G, delta H, delta S, and delta V have been evaluated for the equilibrium.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kornblatt JA,Hui Bon Hoa Gdoi
10.1021/bi00265a009subject
Has Abstractpub_date
1982-10-26 00:00:00pages
5439-44issue
22eissn
0006-2960issn
1520-4995journal_volume
21pub_type
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