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Thermal stability of the polyheme cytochrome c 3 superfamily
Author(s) -
Florens L.,
Bianco P.,
Haladjian J.,
Bruschi M.,
Protasevich I.,
Makarov A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01062-j
Subject(s) - desulfovibrio vulgaris , thermostability , cytochrome , desulfovibrio , cytochrome c , chemistry , crystallography , stereochemistry , biochemistry , biology , enzyme , bacteria , mitochondrion , organic chemistry , genetics , sulfate
The cytochrome c 3 superfamily includes Desulfovibrio polyheme cytochromes c . We report the characteristic thermal stability parameters of the Desulfovibrio desulfuricans Norway ( D.d .N.) cytochromes c 3 ( M r 13,000 and M r 26,000) and the Desulfovibrio vulgaris Hildenborough ( D.v .H.) cytochrome c 3 ( M r 13,000) and high molecular mass cytochrome c (Hmc), as obtained with the help of electronic spectroscopy, voltammetric techniques and differential scanning calorimetry. The polyheme cytochromes are denatured over a wide range of temperatures: the D.v .H. cytochrome c 3 is highly thermostable ( T d = 1°C) contrary to the D.d .N. protein ( T d = 73 C ). The thermostability of the polyheme cytochromes is redox state dependent. The results are discussed in the light of the structural and functional relationships within the cytochrome c 3 superfamily.