Femtosecond spectroscopy of heme proteins

被引：12

作者：

Champion, PM ^{[1
]}

Rosca, F ^{[1
]}

Wang, W ^{[1
]}

Kumar, A ^{[1
]}

Christian, J ^{[1
]}

Demidov, A ^{[1
]}

机构：

[1] Northeastern Univ, Dept Phys, Boston, MA 02115 USA

来源：

LASER TECHNIQUES FOR CONDENSED-PHASE AND BIOLOGICAL SYSTEMS | 1998年 / 3273卷

关键词：

D O I：

10.1117/12.306112

中图分类号：

O43 [光学];

学科分类号：

070207 ; 0803 ;

摘要：

The technique of femtosecond coherence spectroscopy is applied to the heme proteins myoglobin (Mb) and hemoglobin (Hb). Studies of field driven coherences lead to power spectra that are in good agreement with resonance Raman scattering experiments. Studies of the NO bound derivatives of Mb and Kb reveal rapid photolysis and non-radiative relaxation to the ground electronic state. The ensuing nuclear response is oscillatory and displays strong coupling of the NO photolysis reaction to the iron-histidine vibration (at similar to 220 cm(-1)) and to the heme doming mode, which we locate at similar to 40 cm(-1) The doming mode was previously assigned to a mode at similar to 80 cm(-1), which we now believe is actually the first overtone of the doming motion. Other modes at similar to 120 cm(-1) and 160 cm(-1) are also exposed by the new data, suggesting that a progression of doming harmonics is excited due to the strong coupling (i.e., large similar to 0.4 Angstrom iron displacement) of this mode to the photolysis reaction.

引用

页码：80 / 89

页数：10