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Heme d formation in a Shewanella benthica hemoglobin.

Jaime E Martinez Grundman1, Thomas D Schultz1, Jamie L Schlessman2

  • 1T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.

Journal of Inorganic Biochemistry
|July 3, 2024
PubMed
Summary

Shewanella benthica truncated hemoglobin (SbHbN) readily modifies its heme b cofactor into novel heme d derivatives. This unique reactivity, influenced by Tyr34, expands the globin fold

Keywords:
ExtremophileHeme adductHeme dHeme modificationShewanella benthicaTruncated hemoglobin

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbial Physiology

Background:

  • Microbial globins, particularly truncated hemoglobins (HbN), play crucial roles in oxygen transport and metabolism in diverse bacteria.
  • Shewanella benthica is an obligate psychropiezophile, adapted to extreme cold and high-pressure environments, with its HbN (SbHbN) structure being of interest.
  • The active site of globins, specifically the heme environment, dictates their biochemical properties and potential for cofactor modification.

Purpose of the Study:

  • To elucidate the structural and biochemical properties of truncated hemoglobin from Shewanella benthica (SbHbN).
  • To investigate the reactivity of the heme cofactor within the SbHbN active site, particularly under oxidative conditions.
  • To explore the potential for novel heme cofactor formation mediated by the globin fold.

Main Methods:

  • Protein expression and purification of SbHbN.
  • Crystallization of ferric SbHbN and X-ray crystallography to determine its structure.
  • In vitro biochemical assays involving hydrogen peroxide treatment and site-directed mutagenesis (Tyr34Phe replacement).

Main Results:

  • Crystallization of SbHbN revealed a unique heme d derivative with a γ-spirolactone and hydroxyl group, formed over weeks.
  • In solution, hydrogen peroxide treatment led to heme d formation and covalent attachment of heme to the protein.
  • The Tyr34Phe mutation abolished the formation of heme d and the heme-protein covalent linkage, highlighting Tyr34's critical role.

Conclusions:

  • SbHbN exhibits remarkable reactivity, readily modifying its heme b cofactor into novel derivatives like heme d.
  • The tyrosine residue at position 34 (Tyr34) is essential for mediating heme modification and covalent adduct formation.
  • This study demonstrates the globin fold's capacity for supporting diverse heme chemistries, potentially leading to novel cofactor discovery.