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First-Principles Theory of Muon and Muonium Trapping in the Protein Chain of Cytochrome c and Associated Hyperfine Interactions |
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| Authors: | Scheicher R H Cammarere D Briere T M Sahoo N Das T P Pratt F L Nagamine K |
| Institution: | (1) Department of Physics, State University of New York at Albany, Albany, NY 12222, USA;(2) Tamarac High School, Brittenkill, New York, USA;(3) Meson Science Laboratory, High Energy Accelerator Research Organization, Oho 1-1, Tsukuba, Ibaraki 305-0801, Japan;(4) Department of Radiation Oncology, Albany Medical College, Albany, NY 12208, USA;(5) RIKEN-RAL, Didcot, UK;(6) Clarendon Laboratory, Oxford, UK;(7) Muon Science Laboratory, RIKEN (The Institute of Physical and Chemical Research), Wako, Saitama 351-0198, Japan |
| Abstract: | The microscopic details of the electron transfer in cytochrome c (cyt c) are being investigated by the Muon Spin Relaxation (μSR) technique. We are using the Hartree–Fock Cluster Procedure to determine the most likely trapping sites for μ+ and muonium (Mu) in the protein chain, and have performed extensive calculations in single amino acid molecules of the protein chain of cyt c. The double-bonded oxygen atom of the carboxyl group was identified as the trapping site for both μ+ and Mu. Utilizing the wave functions we obtained from the Hartree–Fock calculations, we have determined the hyperfine field that the μ+ in Mu experiences while the latter is trapped at the oxygen. This revised version was published online in September 2006 with corrections to the Cover Date. |
| Keywords: | Hartree– Fock calculations hyperfine properties muon and muonium trapping electron transport biological systems |
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