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Probing the function of heme distortion in the h-nox family

Academic Article
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Overview

authors

  • Olea, C.
  • Boon, E. M.
  • Pellicena, P.
  • Kuriyan, J.
  • Marletta, Michael

publication date

  • 2008

journal

  • ACS Chemical Biology  Journal

abstract

  • Hemoproteins carry out diverse functions utilizing a wide range of chemical reactivity while employing the same heme prosthetic group. It is clear from high-resolution crystal structures and biochemical studies that protein-bound hemes are not planar and adopt diverse conformations. The crystal structure of an H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX) contains the most distorted heme reported to date. In this study, Tt H-NOX was engineered to adopt a flatter heme by mutating proline 115, a conserved residue in the H-NOX family, to alanine. Decreasing heme distortion in Tt H-NOX increases affinity for oxygen and decreases the reduction potential of the heme iron. Additionally, flattening the heme is associated with significant shifts in the N-terminus of the protein. These results show a clear link between the heme conformation and Tt H-NOX structure and demonstrate that heme distortion is an important determinant for maintaining biochemical properties in H-NOX proteins.

subject areas

  • Bacterial Proteins
  • Heme
  • Hemeproteins
  • Molecular Conformation
  • Mutagenesis, Site-Directed
  • Oxygen
  • Protein Binding
  • Protein Conformation
  • Thermoanaerobacter
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Identity

PubMed Central ID

  • PMC2646007

International Standard Serial Number (ISSN)

  • 1554-8929

Digital Object Identifier (DOI)

  • 10.1021/cb800185h

PubMed ID

  • 19032091
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Additional Document Info

start page

  • 703

end page

  • 710

volume

  • 3

issue

  • 11

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