Accession Number : AD0664519

Title :   MOSSBAUER STUDIES OF THE IRON ATOM IN CYTOCHROME C,

Corporate Author : ILLINOIS UNIV URBANA DEPT OF PHYSICS

Personal Author(s) : Cooke,R. ; Debrunner,P.

Report Date : 1967

Pagination or Media Count : 26

Abstract : Mossbauer spectra of the iron atom in horse heart cytochrome c were observed in frozen solution and freeze dried samples for both the oxidized and reduced states. At temperatures above 77K, the spectrum of the oxidized enzyme consisted of a quadrupole split doublet, broadened by a temperature dependent magnetic hyperfine interaction. The spectrum of the reduced enzyme consisted, at all temperatures observed, of two peaks with a quadrupole splitting of 0.12 cm/sec. Upon freeze drying the quadrupole splitting of the oxidized enzyme decreased, whereas the spectrum of the reduced enzyme changed very little. (Author)

Descriptors :   (*ORGANIC PIGMENTS, *MOSSBAUER EFFECT), (*ENZYMES, MOSSBAUER EFFECT), IRON COMPOUNDS, COMPLEX COMPOUNDS, PORPHYRINS, GAMMA RAY SPECTROSCOPY, HYPERFINE STRUCTURE, WAVE FUNCTIONS

Subject Categories : Biochemistry
      Radiation and Nuclear Chemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE