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Histidines 138 and 143 are Copper Binding Ligands in Chromobacterium Violaceum Phenylalanine Hydroxylase

  • Shankar Balasubramanian
  • Robert T. Carr
  • Christopher J. Bender
  • Jack Peisach
  • Stephen J. Benkovic
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 338)

Abstract

Phenylalanine hydroxylase (PAH) from Chromobacterium violaceum (CV) is known to bind an equivalent of divalent copper.1 Studies using pulsed EPR spectroscopy2 have suggested that there are two equatorial imidazoles coordinated to Cu(II) of CV PAH. This observation has been supported by copper-histidine model complexes of the active site3 and more recently by X-ray absorption spectroscopy of the copper containing enzyme.4 We have used a combination of site directed mutagenesis and pulsed EPR spectroscopy to probe the copper binding site of CV PAH and identify the Cu(II) ligands.

Keywords

Wild Type Enzyme Phenylalanine Hydroxylase Chromobacterium Violaceum Divalent Copper Copper Binding Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Shankar Balasubramanian
    • 1
  • Robert T. Carr
    • 1
  • Christopher J. Bender
    • 2
  • Jack Peisach
    • 2
  • Stephen J. Benkovic
    • 1
  1. 1.Department of ChemistryThe Pennsylvania State UniversityUniversity ParkUSA
  2. 2.Department of Molecular PharmacologyAlbert Einstein College of Medicine of Yeshiva UniversityBronxUSA

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