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Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis

Abstract

Porphyromonas gingivalis, a Gram-negative anaerobic bacterium implicated in the development and progression of chronic periodontitis, acquires heme for growth by a novel mechanism composed of HmuY and HmuR proteins. The aim of this study was to characterize the nature of heme binding to HmuY. The protein was expressed, purified and detailed investigations using UV-vis absorption, CD, MCD, and {sup 1}H NMR spectroscopy were carried out. Ferric heme bound to HmuY may be reduced by sodium dithionite and re-oxidized by potassium ferricyanide. Heme complexed to HmuY, with a midpoint potential of 136 mV, is in a low-spin Fe(III) hexa-coordinate environment. Analysis of heme binding to several single and double HmuY mutants with the methionine, histidine, cysteine, or tyrosine residues replaced by an alanine residue identified histidines 134 and 166 as potential heme ligands.
Authors:
Wojtowicz, Halina; [1]  Wojaczynski, Jacek; [2]  Olczak, Mariusz; [1]  Kroliczewski, Jaroslaw; [3]  Latos-Grazynski, Lechoslaw; [2]  Olczak, Teresa [1] 
  1. Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Tamka 2, 50-137 Wroclaw (Poland)
  2. Department of Chemistry, University of Wroclaw, 50-383 Wroclaw (Poland)
  3. Laboratory of Biophysics, Faculty of Biotechnology, University of Wroclaw, 50-148 Wroclaw (Poland)
Publication Date:
May 29, 2009
Product Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 383; Journal Issue: 2; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Subject:
60 APPLIED LIFE SCIENCES; ALANINES; CYSTEINE; FERRICYANIDES; HEME; HISTIDINE; MAGNETIC CIRCULAR DICHROISM; METHIONINE; NUCLEAR MAGNETIC RESONANCE; TYROSINE
OSTI ID:
22199704
Country of Origin:
United States
Language:
English
Other Identifying Numbers:
Journal ID: ISSN 0006-291X; CODEN: BBRCA9; Other: PII: S0006-291X(09)00648-2; TRN: US09R1693020527
Availability:
Available from http://dx.doi.org/10.1016/j.bbrc.2009.03.148
Submitting Site:
USN
Size:
page(s) 178-182
Announcement Date:
Feb 27, 2014

Citation Formats

Wojtowicz, Halina, Wojaczynski, Jacek, Olczak, Mariusz, Kroliczewski, Jaroslaw, Latos-Grazynski, Lechoslaw, and Olczak, Teresa. Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis. United States: N. p., 2009. Web. doi:10.1016/J.BBRC.2009.03.148.
Wojtowicz, Halina, Wojaczynski, Jacek, Olczak, Mariusz, Kroliczewski, Jaroslaw, Latos-Grazynski, Lechoslaw, & Olczak, Teresa. Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis. United States. doi:10.1016/J.BBRC.2009.03.148.
Wojtowicz, Halina, Wojaczynski, Jacek, Olczak, Mariusz, Kroliczewski, Jaroslaw, Latos-Grazynski, Lechoslaw, and Olczak, Teresa. 2009. "Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis." United States. doi:10.1016/J.BBRC.2009.03.148. https://www.osti.gov/servlets/purl/10.1016/J.BBRC.2009.03.148.
@misc{etde_22199704,
title = {Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis}
author = {Wojtowicz, Halina, Wojaczynski, Jacek, Olczak, Mariusz, Kroliczewski, Jaroslaw, Latos-Grazynski, Lechoslaw, and Olczak, Teresa}
abstractNote = {Porphyromonas gingivalis, a Gram-negative anaerobic bacterium implicated in the development and progression of chronic periodontitis, acquires heme for growth by a novel mechanism composed of HmuY and HmuR proteins. The aim of this study was to characterize the nature of heme binding to HmuY. The protein was expressed, purified and detailed investigations using UV-vis absorption, CD, MCD, and {sup 1}H NMR spectroscopy were carried out. Ferric heme bound to HmuY may be reduced by sodium dithionite and re-oxidized by potassium ferricyanide. Heme complexed to HmuY, with a midpoint potential of 136 mV, is in a low-spin Fe(III) hexa-coordinate environment. Analysis of heme binding to several single and double HmuY mutants with the methionine, histidine, cysteine, or tyrosine residues replaced by an alanine residue identified histidines 134 and 166 as potential heme ligands.}
doi = {10.1016/J.BBRC.2009.03.148}
journal = {Biochemical and Biophysical Research Communications}
issue = {2}
volume = {383}
journal type = {AC}
place = {United States}
year = {2009}
month = {May}
}