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Light induced states in MbCO denatured with Guanidine hydrochloride

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Abstract

We present the results of a comparative study of the binding of carbon monoxide to myoglobin in glycerol/buffer solution with different concentrations of guanidine hydrochloride, under extended illumination over the temperature range 30 – 80 K. The changes in the Soret band indicate that the folding state of the protein is a key parameter in determining the photodissociation process and the relaxation rate of the protein.

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Authors and Affiliations

  1. Dipartimento di Fisica and Istituto Nazionale di Fisica della Materia, Universita' “La Sapienza”, I-00185 Roma, Italy, , , , , , IT

    Francesca Natali, Lucia Moretti, Federico Boffi, Antonio Bianconi & A. Congiu Castellano

  2. Dipartimento di Medicina Sperimentale, Universita' dell'Aquila, I-67100 L'Aquila, Italy, , , , , , IT

    Stefano Della Longa

Authors
  1. Francesca Natali
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  2. Lucia Moretti
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  3. Federico Boffi
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  4. Antonio Bianconi
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  5. Stefano Della Longa
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  6. A. Congiu Castellano
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Additional information

Received: 30 January 1997 / Accepted: 14 August 1997

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Natali, F., Moretti, L., Boffi, F. et al. Light induced states in MbCO denatured with Guanidine hydrochloride. Eur Biophys J 27, 1–7 (1998). https://doi.org/10.1007/s002490050104

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  • DOI: https://doi.org/10.1007/s002490050104

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