Electron spin-lattice relaxation rates for high-spin Fe(III) complexes in glassy solvents at temperatures between 6 and 298 K.
The temperature dependence of spin-lattice relaxation rates was analyzed for four high-spin nonheme iron proteins between 5 and 20 K, for three high-spin iron porphyrins between 5 and 118 K, and for four high-spin heme proteins between 5 and 150 to 298 K. For the nonheme proteins the zero-field splittings, D, are less than 0.7 cm(-1), and the relaxation is dominated by the Orbach and Raman processes. For the iron porphyrins and heme proteins D is between 4 and 12 cm(-1) and the relaxation is dominated by the Orbach process between about 5 and 100 K and by a local mode at higher temperatures. The relaxation rates for the heme proteins in glassy matrices extrapolated to values at room temperature that are similar to values obtained by NMR relaxivity in fluid solution. This similarity suggests that for high-spin Fe(III) heme proteins with effective intramolecular spin-lattice relaxation processes, the additional motional freedom gained when a relatively large protein goes from glassy solid to liquid solution at room temperature has little impact on spin-lattice relaxation.
Zhou
Y
Y
Department of Chemistry and Biochemistry, University of Denver, Colorado 80208, USA.
Bowler
B E
BE
Eaton
G R
GR
Eaton
S S
SS
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D005898:Glass; D006420:Hemeproteins / Q000737:chemistry*; D058085:Iron Compounds / Q000737:chemistry*; D008433:Mathematics; D008665:Metalloporphyrins / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry; D012997:Solvents; D013113:Spin Labels; D013696:Temperature
D006420:Hemeproteins; D058085:Iron Compounds; D008665:Metalloporphyrins; D011506:Proteins; D012997:Solvents; D013113:Spin Labels