MOSSBAUER STUDIES OF THE IRON ATOM IN CYTOCHROME C,
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)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1967
- Accession Number
- AD0664519
Entities
People
- P. Debrunner
- R. Cooke
Organizations
- University of Illinois Urbana–Champaign