Different relaxations in myoglobin after photolysis

Proceedings of the National Academy of Sciences of the United States of America
Matteo LevantinoP Ormos

Abstract

To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration in myoglobin (Mb), we measured time-resolved absorption spectra in the Soret region after photolysis of carbon monoxide Mb (MbCO) in the temperature interval 120-260 K and in the time window 350 ns to 200 ms. The spectral contributions of both photolyzed (Mb*) and liganded Mb (MbCO) have been analyzed by taking into account homogeneous bandwidth, coupling to vibrational modes, and static conformational heterogeneity. We succeeded in separating the "time-dependent" spectral changes, and this work provides possibilities to identify the events in the process of ligand rebinding. KHB is dominant at T <190 K in both the Mb* and the MbCO components. For MbCO, conformational substates interconversion at higher temperatures tends to average out the KHB effect. At 230-260 K, whereas almost no shift is observed in the MbCO spectrum, a shift of the order of approximately 80 cm(-1) is observed in Mb*. We attribute this shift to protein relaxation coupled to ligand migration. The time dependence of the Mb* spectral shift is interpreted with a model that enables us to calculate the highly nonexponential relaxation kinetics. Fits of stretched e...Continue Reading

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Citations

Oct 16, 2003·Toxicon : Official Journal of the International Society on Toxinology·Ursula Castro de OliveiraPaulo Lee Ho
Jul 17, 2009·Journal of the American Chemical Society·Feng Guo, Joel M Friedman
Feb 4, 2010·Journal of the American Chemical Society·Abdelkrim BenabbasPaul M Champion
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Oct 7, 2017·Journal of the American Chemical Society·Abdelkrim BenabbasPaul M Champion
Nov 6, 2013·Biochemistry·Mario Compiani, Emidio Capriotti

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