HEAT STABILIZATION DEPENDENCE ON REDOX STATE OF CYTOCHROME-CD1 OXIDASE FROM PSEUDOMONAS-AERUGINOSA

被引:5
作者
MITRA, S [1 ]
DONOVAN, JW [1 ]
BERSOHN, R [1 ]
机构
[1] USDA SEA, WESTERN REG RES CTR, BERKELEY, CA 94710 USA
关键词
D O I
10.1016/0006-291X(81)91880-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The irreversible thermal denaturation of cytochrome cd1 oxidase from P. aeruginosa as a function of the oxidation-reduction states of its hemes was observed with a differential scanning calorimeter. Upon full reduction of the 4 hemes, the apparent denaturation temperature decreases by .apprx. 10.degree. C and the denaturation enthalpy decreases slightly: oxidized, 5.9 cal/g; reduced, 5.4 cal/g. At pH 7.5, the first order rate constants for denaturation at 90.degree. C are: reduced, 33 .times. 10-3 s-1; oxidized, 3 .times. 10-3 s-1. Oxidation of the hemes results in heat stabilization of the cytochrome oxidase. The activation energy for denaturation of fully reduced oxidase, 53 kcal/mol, is less than that for fully oxidized protein (73 kcal/mol).
引用
收藏
页码:140 / 146
页数:7
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