CORRELATION BETWEEN THE OPTICAL AND MAGNETIC PROPERTIES OF FERRIC N-ACETYLATED HEME OCTAPEPTIDE COMPLEXES
Journal Article
·
· Interaction between Iron and Proteins in Oxygen and Electron Transport
OSTI ID:1070084
The room temperature magnetic susceptibility of the complexes of the ferric N-acetylated heme octapeptide (N-H8PT) from horse heart cytochrome c is known to be generally consistent with the absorption and magnetic circular dichroism (MCD) spectra of these complexes. However, the N-acetylated methionine complex of the N-H8PT, which has axial coordination identical to that of the parent molecule, is found to exhibit a thermal mixture of high spin (S=5/2) and low spin (S=1/2) states. The temperature dependence of the magnetic susceptibility of the N-acetylmethionine complex yields {Delta}H{sup 0} = -7.6kca1/mole and {Delta}S° = -25.9 e.u. for a high to low spin transition. The electron spin resonance (ESR) spectrum of the N-acetylmethionine complex indicates a low spin ground state, with g values at 1.51, 2.31, and 2.91, which are distinct from those of cytochrome c. The axial ({Delta}) and rhombic (V) distortion parameters of the {sup 2}T{sub 2g} state correspond to 2.96{lambda} and 1.94{lambda}, respectively, where {lambda} is the spin-orbit coupling constant. A model is proposed to account for the uniqueness of the N-acetylmethionine complex: a change in the Fe-S distance may play a role in regulating the redox properties of cytochrome c.
- Research Organization:
- Ernest Orlando Lawrence Berkeley National Laboratory, Berkeley, CA (US)
- Sponsoring Organization:
- Chemical Sciences Division
- DOE Contract Number:
- AC02-05CH11231
- OSTI ID:
- 1070084
- Report Number(s):
- LBL-11015
- Journal Information:
- Interaction between Iron and Proteins in Oxygen and Electron Transport, Journal Name: Interaction between Iron and Proteins in Oxygen and Electron Transport
- Country of Publication:
- United States
- Language:
- English
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