First-principle determination of muon and muonium trapping sites in horse heart cytochrome c and investigation of magnetic hyperfine properties

The trapping of the muon in the heme unit and of the muon and muonium in amino acids on the protein chain in horse heart cytochrome c are studied using the Hartree–Fock–Roothaan procedure for the interpretation of resonance data from μSR experiments. For the heme unit, trapping of the muon has been...

Full description

Saved in:
Bibliographic Details
Published in:Physica. B, Condensed matter Condensed matter, 2000-08, Vol.289, p.636-639
Main Authors: Cammarere, D, Scheicher, R.H, Sahoo, N, Das, T.P, Nagamine, K
Format: Article
Language:English
Subjects:
Biological systems
Electron transport
Hartree–Fock calculations
Hyperfine properties
Muon and muonium trapping
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The trapping of the muon in the heme unit and of the muon and muonium in amino acids on the protein chain in horse heart cytochrome c are studied using the Hartree–Fock–Roothaan procedure for the interpretation of resonance data from μSR experiments. For the heme unit, trapping of the muon has been found at the nitrogen of the pyrrole ring with an expected μSR shift of 88.4 ppm. For the amino acids on the protein chain, studies of cystein, lysine and alanine show that the muon attaches itself to all atoms carrying negative effective charges including the oxygen of the CO group which exists in all amino acids, the oxygen and carbon trapping the muonium through the break up of the π bond between them.
ISSN:0921-4526
1873-2135
DOI:10.1016/S0921-4526(00)00299-4