Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins

Mario Milani; Alessandra Pesce; Marco Nardini; Hugues Ouellet; Yannick Ouellet; Sylvia Dewilde; Alessio Bocedi; Paolo Ascenzi; Michel Guertin; Luc Moens; Joel M. Friedman; Jonathan B. Wittenberg; Martino Bolognesi

doi:10.1016/j.jinorgbio.2004.10.035

Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins

Mario Milani, Alessandra Pesce, Marco Nardini, Hugues Ouellet, Yannick Ouellet, Sylvia Dewilde, Alessio Bocedi, Paolo Ascenzi, Michel Guertin, Luc Moens, Joel M. Friedman, Jonathan B. Wittenberg, Martino Bolognesi

Physiology & Biophysics

Research output: Contribution to journal › Article

104 Scopus citations

Abstract

Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed in eubacteria, cyanobacteria, unicellular eukaryotes, and in higher plants, constituting a distinct group within the hemoglobin (Hb) superfamily. TrHbs display amino acid sequences 20-40 residues shorter than classical (non)vertebrate Hbs and myoglobins, to which they are scarcely related by sequence similarity. The trHb tertiary structure is based on a 2-on-2 α-helical sandwich, which represents a striking editing of the highly conserved 3-on-3 α-helical globin fold, achieved through deletion/truncation of α-helices and specific residue substitutions. Despite their 'minimal' polypeptide chain span, trHbs display an inner tunnel/cavity system held to support ligand diffusion to/from the heme distal pocket, accumulation of heme ligands within the protein matrix, and/or multiligand reactions. Moreover, trHbs bind and effectively stabilize the heme and recognize diatomic ligands (i.e., O₂, CO, NO, and cyanide), albeit with varying thermodynamic and kinetic parameters. Here, structural bases for heme binding and diatomic ligand recognition by trHbs are reviewed.

Original language	English (US)
Pages (from-to)	97-109
Number of pages	13
Journal	Journal of Inorganic Biochemistry
Volume	99
Issue number	1
DOIs	https://doi.org/10.1016/j.jinorgbio.2004.10.035
State	Published - Jan 2005

Keywords

Diatomic ligand recognition
Heme stabilization
Hemoglobin
Myoglobin
Protein cavities
Truncated hemoglobin

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

Access to Document

10.1016/j.jinorgbio.2004.10.035

Fingerprint Dive into the research topics of 'Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins'. Together they form a unique fingerprint.

Cite this

Milani, M., Pesce, A., Nardini, M., Ouellet, H., Ouellet, Y., Dewilde, S., Bocedi, A., Ascenzi, P., Guertin, M., Moens, L., Friedman, J. M., Wittenberg, J. B., & Bolognesi, M. (2005). Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins. Journal of Inorganic Biochemistry, 99(1), 97-109. https://doi.org/10.1016/j.jinorgbio.2004.10.035

Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins. / Milani, Mario; Pesce, Alessandra; Nardini, Marco; Ouellet, Hugues; Ouellet, Yannick; Dewilde, Sylvia; Bocedi, Alessio; Ascenzi, Paolo; Guertin, Michel; Moens, Luc; Friedman, Joel M.; Wittenberg, Jonathan B.; Bolognesi, Martino.

In: Journal of Inorganic Biochemistry, Vol. 99, No. 1, 01.2005, p. 97-109.

Research output: Contribution to journal › Article

Milani, Mario ; Pesce, Alessandra ; Nardini, Marco ; Ouellet, Hugues ; Ouellet, Yannick ; Dewilde, Sylvia ; Bocedi, Alessio ; Ascenzi, Paolo ; Guertin, Michel ; Moens, Luc ; Friedman, Joel M. ; Wittenberg, Jonathan B. ; Bolognesi, Martino. / Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins. In: Journal of Inorganic Biochemistry. 2005 ; Vol. 99, No. 1. pp. 97-109.

@article{597d219c0aeb431a8c010c86d395f055,

title = "Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins",

abstract = "Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed in eubacteria, cyanobacteria, unicellular eukaryotes, and in higher plants, constituting a distinct group within the hemoglobin (Hb) superfamily. TrHbs display amino acid sequences 20-40 residues shorter than classical (non)vertebrate Hbs and myoglobins, to which they are scarcely related by sequence similarity. The trHb tertiary structure is based on a 2-on-2 α-helical sandwich, which represents a striking editing of the highly conserved 3-on-3 α-helical globin fold, achieved through deletion/truncation of α-helices and specific residue substitutions. Despite their 'minimal' polypeptide chain span, trHbs display an inner tunnel/cavity system held to support ligand diffusion to/from the heme distal pocket, accumulation of heme ligands within the protein matrix, and/or multiligand reactions. Moreover, trHbs bind and effectively stabilize the heme and recognize diatomic ligands (i.e., O2, CO, NO, and cyanide), albeit with varying thermodynamic and kinetic parameters. Here, structural bases for heme binding and diatomic ligand recognition by trHbs are reviewed.",

keywords = "Diatomic ligand recognition, Heme stabilization, Hemoglobin, Myoglobin, Protein cavities, Truncated hemoglobin",

author = "Mario Milani and Alessandra Pesce and Marco Nardini and Hugues Ouellet and Yannick Ouellet and Sylvia Dewilde and Alessio Bocedi and Paolo Ascenzi and Michel Guertin and Luc Moens and Friedman, {Joel M.} and Wittenberg, {Jonathan B.} and Martino Bolognesi",

year = "2005",

month = jan,

doi = "10.1016/j.jinorgbio.2004.10.035",

language = "English (US)",

volume = "99",

pages = "97--109",

journal = "Journal of Inorganic Biochemistry",

issn = "0162-0134",

publisher = "Elsevier Inc.",

number = "1",

}

TY - JOUR

T1 - Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins

AU - Milani, Mario

AU - Pesce, Alessandra

AU - Nardini, Marco

AU - Ouellet, Hugues

AU - Ouellet, Yannick

AU - Dewilde, Sylvia

AU - Bocedi, Alessio

AU - Ascenzi, Paolo

AU - Guertin, Michel

AU - Moens, Luc

AU - Friedman, Joel M.

AU - Wittenberg, Jonathan B.

AU - Bolognesi, Martino

PY - 2005/1

Y1 - 2005/1

N2 - Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed in eubacteria, cyanobacteria, unicellular eukaryotes, and in higher plants, constituting a distinct group within the hemoglobin (Hb) superfamily. TrHbs display amino acid sequences 20-40 residues shorter than classical (non)vertebrate Hbs and myoglobins, to which they are scarcely related by sequence similarity. The trHb tertiary structure is based on a 2-on-2 α-helical sandwich, which represents a striking editing of the highly conserved 3-on-3 α-helical globin fold, achieved through deletion/truncation of α-helices and specific residue substitutions. Despite their 'minimal' polypeptide chain span, trHbs display an inner tunnel/cavity system held to support ligand diffusion to/from the heme distal pocket, accumulation of heme ligands within the protein matrix, and/or multiligand reactions. Moreover, trHbs bind and effectively stabilize the heme and recognize diatomic ligands (i.e., O2, CO, NO, and cyanide), albeit with varying thermodynamic and kinetic parameters. Here, structural bases for heme binding and diatomic ligand recognition by trHbs are reviewed.

AB - Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed in eubacteria, cyanobacteria, unicellular eukaryotes, and in higher plants, constituting a distinct group within the hemoglobin (Hb) superfamily. TrHbs display amino acid sequences 20-40 residues shorter than classical (non)vertebrate Hbs and myoglobins, to which they are scarcely related by sequence similarity. The trHb tertiary structure is based on a 2-on-2 α-helical sandwich, which represents a striking editing of the highly conserved 3-on-3 α-helical globin fold, achieved through deletion/truncation of α-helices and specific residue substitutions. Despite their 'minimal' polypeptide chain span, trHbs display an inner tunnel/cavity system held to support ligand diffusion to/from the heme distal pocket, accumulation of heme ligands within the protein matrix, and/or multiligand reactions. Moreover, trHbs bind and effectively stabilize the heme and recognize diatomic ligands (i.e., O2, CO, NO, and cyanide), albeit with varying thermodynamic and kinetic parameters. Here, structural bases for heme binding and diatomic ligand recognition by trHbs are reviewed.

KW - Diatomic ligand recognition

KW - Heme stabilization

KW - Hemoglobin

KW - Myoglobin

KW - Protein cavities

KW - Truncated hemoglobin

UR - http://www.scopus.com/inward/record.url?scp=10444229578&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=10444229578&partnerID=8YFLogxK

U2 - 10.1016/j.jinorgbio.2004.10.035

DO - 10.1016/j.jinorgbio.2004.10.035

M3 - Article

C2 - 15598494

AN - SCOPUS:10444229578

VL - 99

SP - 97

EP - 109

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 1

ER -