A cascade through spin states in the ultrafast haem relaxation of met-myoglobin

We report on a study of the early relaxation processes of met-Myoglobin in aqueous solution, using a combination of ultrafast broadband fluorescence detection and transient absorption with a broad UV-visible continuum probe at different pump energies. Reconstruction of the spectra of the transient s...

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Bibliographic Details
Published in:The Journal of chemical physics 2014-01, Vol.140 (2), p.025103-025103
Main Authors: Consani, Cristina, Auböck, Gerald, Bräm, Olivier, van Mourik, Frank, Chergui, Majed
Format: Article
Language:English
Subjects:
ABSORPTION
AQUEOUS SOLUTIONS
Broadband
DETECTION
FLUORESCENCE
GROUND STATES
Haem
Heme - chemistry
INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY
IRON
Iron - chemistry
Metmyoglobin - chemistry
MYOGLOBIN
Myoglobins
PHOTOLYSIS
Porphyrins - chemistry
RELAXATION
SPECTRA
Spectrometry, Fluorescence
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Summary:We report on a study of the early relaxation processes of met-Myoglobin in aqueous solution, using a combination of ultrafast broadband fluorescence detection and transient absorption with a broad UV-visible continuum probe at different pump energies. Reconstruction of the spectra of the transient species unravels the details of the haem photocycle in the absence of photolysis. Besides identifying a branching in the ultrafast relaxation of the haem, we show clear evidence for an electronic character of the intermediates, contrary to the commonly accepted idea that the early time relaxation of the haem is only due to cooling. The decay back to the ground state proceeds partially as a cascade through iron spin states, which seems to be a general characteristic of haem systems.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.4861467