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• W2085641569 endingPage "140" @default.
• W2085641569 startingPage "131" @default.
• W2085641569 abstract "Photodissociation of carbon monoxide myoglobin (MbCO) creates Mb in nonequilibrium conformation and triggers a global conformational charge. The driving force for the change is localized initially in the iron-porhyrin coordinate. The dynamics of the iron-prophyrin displacement at physiologically relevant temperatures have been followed by probing the evolution of band III, a weak iron-prophyrin charge-transfer transition near 13110 cmt-1 (763 nm) that is sensitive to the out-of-plane position of the iron. This functionally important motion is highly nonexponential, stretching over 5 decades in time in 70:30 (w/w) glycerol/water mixtures at 301 ±1 K. The relaxation is well described by a stretched exponential function that has been modified to account for the limiting rate associated with the primary relaxation process." @default.
• W2085641569 created "2016-06-24" @default.
• W2085641569 creator A5010563919 @default.
• W2085641569 creator A5068835223 @default.
• W2085641569 creator A5073859299 @default.
• W2085641569 date "1994-03-01" @default.
• W2085641569 modified "2023-09-27" @default.
• W2085641569 title "Complex nonexponential relaxation in myoglobin after photodissociation of MbCO: measurement and analysis from 2 ps to 56 υs" @default.
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• W2085641569 doi "https://doi.org/10.1016/0301-0104(93)e0414-q" @default.
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