Molecular bases for heme: ligand recognition in sperm whale (Physeter Catodon) and Aplysia limacine myoglobin

Menico Rizzi; Paolo Ascenzi; Alessandro Coda; Maurizio Brunori; Martino Bolognesi

doi:10.1007/BF03001186

Molecular bases for heme: ligand recognition in sperm whale (Physeter Catodon) and Aplysia limacine myoglobin

Menico Rizzi, Paolo Ascenzi, Alessandro Coda, Maurizio Brunori, Martino Bolognesi

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

Research output: Contribution to journal › Article › peer-review

Abstract

The crystal structure of sperm whale myoglobin (Mb):azide complex has been determined and refined at 1.8 Å resolution. The ligand is coordinated to the heme iron, and deeply buried in the inner part of the distal site. The structural organization of this complex differs substantially from that observed in A. limacina Mb: azide complex, in which the iron coordinated ligand is directed towards the outer solvent region of the protein. In the case of sperm whale Mb the bound ligand is stabilized by a hydrogen bond to residue HisE7; in the case of A. limacina Mb the ligand is directly hydrogen bonded to ArgE10. The structures of the complexes described underline different mechanisms of ligand recognition and stabilization in the two Mb's, and allow a rational interpretation of the different kinetic and thermodynamic properties observed in globins lacking a polar residue at the distal E7 site.

Original language	English
Pages (from-to)	65-73
Number of pages	9
Journal	Rendiconti Lincei
Volume	4
Issue number	1
DOIs	https://doi.org/10.1007/BF03001186
Publication status	Published - Mar 1993

Keywords

Biocrystallography: Protein:ligand interactions
Heme proteins
Myoglobin
Protein structure

ASJC Scopus subject areas

Engineering(all)
Environmental Science(all)
Earth and Planetary Sciences(all)
Agricultural and Biological Sciences(all)

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10.1007/BF03001186

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title = "Molecular bases for heme: ligand recognition in sperm whale (Physeter Catodon) and Aplysia limacine myoglobin",

abstract = "The crystal structure of sperm whale myoglobin (Mb):azide complex has been determined and refined at 1.8 {\AA} resolution. The ligand is coordinated to the heme iron, and deeply buried in the inner part of the distal site. The structural organization of this complex differs substantially from that observed in A. limacina Mb: azide complex, in which the iron coordinated ligand is directed towards the outer solvent region of the protein. In the case of sperm whale Mb the bound ligand is stabilized by a hydrogen bond to residue HisE7; in the case of A. limacina Mb the ligand is directly hydrogen bonded to ArgE10. The structures of the complexes described underline different mechanisms of ligand recognition and stabilization in the two Mb's, and allow a rational interpretation of the different kinetic and thermodynamic properties observed in globins lacking a polar residue at the distal E7 site.",

keywords = "Biocrystallography: Protein:ligand interactions, Heme proteins, Myoglobin, Protein structure",

author = "Menico Rizzi and Paolo Ascenzi and Alessandro Coda and Maurizio Brunori and Martino Bolognesi",

year = "1993",

month = mar,

doi = "10.1007/BF03001186",

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pages = "65--73",

journal = "ATTI Della Accademia Nazionale Dei Lincei Rendiconti Lincei Scienze Fisiche E Naturali",

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publisher = "Accademia Nazionale dei Lincei",

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TY - JOUR

T1 - Molecular bases for heme

T2 - ligand recognition in sperm whale (Physeter Catodon) and Aplysia limacine myoglobin

AU - Rizzi, Menico

AU - Ascenzi, Paolo

AU - Coda, Alessandro

AU - Brunori, Maurizio

AU - Bolognesi, Martino

PY - 1993/3

Y1 - 1993/3

N2 - The crystal structure of sperm whale myoglobin (Mb):azide complex has been determined and refined at 1.8 Å resolution. The ligand is coordinated to the heme iron, and deeply buried in the inner part of the distal site. The structural organization of this complex differs substantially from that observed in A. limacina Mb: azide complex, in which the iron coordinated ligand is directed towards the outer solvent region of the protein. In the case of sperm whale Mb the bound ligand is stabilized by a hydrogen bond to residue HisE7; in the case of A. limacina Mb the ligand is directly hydrogen bonded to ArgE10. The structures of the complexes described underline different mechanisms of ligand recognition and stabilization in the two Mb's, and allow a rational interpretation of the different kinetic and thermodynamic properties observed in globins lacking a polar residue at the distal E7 site.

AB - The crystal structure of sperm whale myoglobin (Mb):azide complex has been determined and refined at 1.8 Å resolution. The ligand is coordinated to the heme iron, and deeply buried in the inner part of the distal site. The structural organization of this complex differs substantially from that observed in A. limacina Mb: azide complex, in which the iron coordinated ligand is directed towards the outer solvent region of the protein. In the case of sperm whale Mb the bound ligand is stabilized by a hydrogen bond to residue HisE7; in the case of A. limacina Mb the ligand is directly hydrogen bonded to ArgE10. The structures of the complexes described underline different mechanisms of ligand recognition and stabilization in the two Mb's, and allow a rational interpretation of the different kinetic and thermodynamic properties observed in globins lacking a polar residue at the distal E7 site.

KW - Biocrystallography: Protein:ligand interactions

KW - Heme proteins

KW - Myoglobin

KW - Protein structure

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JF - ATTI Della Accademia Nazionale Dei Lincei Rendiconti Lincei Scienze Fisiche E Naturali

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