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XANES of carboxy and cyanomet-myoglobin The role of the distal histidine in the bent Fe−C−O configuration

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Abstract

The ligand bonding geometry of carboxy-and cyanomet-myoglobin (MbCO and MbCN) has been measured by the XANES method (X-ray Absorption Near Edge Structure). A comparison between the ligand bonding geometry of carboxy- and cyanomet-myoglobin and of chelated protoheme methyl ester shows that the bent Fe−C−O configuration is the same in both systems. Therefore, we suggest that this configuration is not associated with any steric contraint imposed by the side chains of the aminoacid residues at the distal side of the heme pocket.

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Authors and Affiliations

  1. Dipartimento di Fisica, Università “La Sapienza”, I-00185, Roma, Italy

    A. Bianconi, A. Congiu-Castellano & M. Dell'Ariccia

  2. Laboratori Nazionali di Frascati, CNR-INFN, I-00044, Frascati (Roma), Italy

    E. Burattini

  3. Daresbury Laboratory, SERC, Daresbury, WA4 4AD, Warrington, UK

    P. J. Durham

  4. Dipartimento di Biologia, Università di Padova, I-35131, Padova, Italy

    G. M. Giacometti

Authors
  1. A. Bianconi
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  2. A. Congiu-Castellano
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  3. A. Giovannelli
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  4. M. Dell'Ariccia
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  5. E. Burattini
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  6. P. J. Durham
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  7. G. M. Giacometti
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Bianconi, A., Congiu-Castellano, A., Giovannelli, A. et al. XANES of carboxy and cyanomet-myoglobin The role of the distal histidine in the bent Fe−C−O configuration. Eur Biophys J 14, 7–10 (1986). https://doi.org/10.1007/BF00260397

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  • DOI: https://doi.org/10.1007/BF00260397

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