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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 languageEnglish
Pages (from-to)65-73
Number of pages9
JournalRendiconti Lincei
Volume4
Issue number1
DOIs
Publication statusPublished - Mar 1993

Fingerprint

Sperm Whale
Aplysia
myoglobin
Myoglobin
heme
Heme
whale
sperm
ligand
Ligands
azides
Azides
hydrogen
Hydrogen
Iron
heme iron
iron
Globins
thermodynamic property
crystal structure

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)

Cite this

Molecular bases for heme : ligand recognition in sperm whale (Physeter Catodon) and Aplysia limacine myoglobin. / Rizzi, Menico; Ascenzi, Paolo; Coda, Alessandro; Brunori, Maurizio; Bolognesi, Martino.

In: Rendiconti Lincei, Vol. 4, No. 1, 03.1993, p. 65-73.

Research output: Contribution to journalArticle

Rizzi, Menico ; Ascenzi, Paolo ; Coda, Alessandro ; Brunori, Maurizio ; Bolognesi, Martino. / Molecular bases for heme : ligand recognition in sperm whale (Physeter Catodon) and Aplysia limacine myoglobin. In: Rendiconti Lincei. 1993 ; Vol. 4, No. 1. pp. 65-73.
@article{54e0786eb82245bb83384c5ba17db875,
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 = "3",
doi = "10.1007/BF03001186",
language = "English",
volume = "4",
pages = "65--73",
journal = "ATTI Della Accademia Nazionale Dei Lincei Rendiconti Lincei Scienze Fisiche E Naturali",
issn = "2037-4631",
publisher = "Accademia Nazionale dei Lincei",
number = "1",

}

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

UR - http://www.scopus.com/inward/record.url?scp=0002978901&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0002978901&partnerID=8YFLogxK

U2 - 10.1007/BF03001186

DO - 10.1007/BF03001186

M3 - Article

VL - 4

SP - 65

EP - 73

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

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

SN - 2037-4631

IS - 1

ER -