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Structural determinants of ligand binding in truncated hemoglobins: Resonance Raman spectroscopy of the native states and their carbon monoxide and hydroxide complexes.

Authors
  • Feis, Alessandro1
  • Howes, Barry D1
  • Milazzo, Lisa1
  • Coppola, Daniela2
  • Smulevich, Giulietta1
  • 1 Dipartimento di Chimica "Ugo Schiff,", Università di Firenze, Via della Lastruccia 3-13, Sesto Fiorentino, 50019, Italy. , (Italy)
  • 2 Dipartimento di Scienze bio-agroalimentari del CNR (DiSBA-CNR), CNR, Via Pietro Castellino 111, Naples, I-80131, Italy. , (Italy)
Type
Published Article
Journal
Biopolymers
Publisher
Wiley (John Wiley & Sons)
Publication Date
Aug 01, 2018
Volume
109
Issue
10
Identifiers
DOI: 10.1002/bip.23114
PMID: 29603146
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The ligand binding characteristics of heme-containing proteins are determined by a number of factors, including the nature and conformation of the distal residues and their capability to stabilize the heme-bound ligand via hydrogen-bonding and electrostatic interactions. In this regard, the heme pockets of truncated hemoglobins (TrHbs) constitute an interesting case study as they share many common features, including a number of polar cavity residues. In this review, we will focus on three proteins of group II TrHbs, from Thermobifida fusca (Tf-HbO) and Pseudoalteromonas haloplanktis TAC125 (Ph-HbO). Although the residues in positions G8 (Trp) and B10 (Tyr) are conserved in all three proteins, the CD1 residue is a Tyr in T. fusca and a His in P. haloplanktis. Comparison of the ligand binding characteristics of these proteins, in particular the hydroxo and CO ligands by means of resonance Raman spectroscopy, reveals that this single difference in the key heme cavity residues markedly affects their ligand binding capability and conformation. Furthermore, although the two Ph-HbOs (Ph-HbO-2217 and Ph-HbO-0030) have identical key cavity residues, they display distinct ligand binding properties. © 2018 Wiley Periodicals, Inc.

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