Sulfur K-Edge XAS and DFT Calculations on NitrileHydratase: Geometric and Electronic Structure of the Non-heme Iron Active Site Metadata

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Title

  • Main Title Sulfur K-Edge XAS and DFT Calculations on NitrileHydratase: Geometric and Electronic Structure of the Non-heme Iron Active Site

Creator

  • Author: Dey, Abhishek
    Creator Type: Personal
  • Author: Chow, Marina
    Creator Type: Personal
  • Author: /Stanford U., Chem. Dept.
    Creator Type: Personal
  • Author: Taniguchi, Kayoko
    Creator Type: Personal
  • Author: /Wako, RIKEN
    Creator Type: Personal
  • Author: Lugo-Mas, Priscilla
    Creator Type: Personal
  • Author: Davin, Steven
    Creator Type: Personal
  • Author: /Washington U., Seattle
    Creator Type: Personal
  • Author: Maeda, Mizuo
    Creator Type: Personal
  • Author: /SLAC, SSRL
    Creator Type: Personal
  • Author: Kovacs, Julie A.
    Creator Type: Personal
  • Author: /Washington U., Seattle
    Creator Type: Personal
  • Author: Odaka, Masafumi
    Creator Type: Personal
  • Author: /Wako, RIKEN
    Creator Type: Personal
  • Author: Hodgson, Keith O.
    Creator Type: Personal
  • Author: Hedman, Britt
    Creator Type: Personal
  • Author: Solomon, Edward I.
    Creator Type: Personal
  • Author: /SLAC, SSRL
    Creator Type: Personal

Contributor

  • Sponsor: United States. Department of Energy.
    Contributor Type: Organization

Publisher

  • Name: Stanford Linear Accelerator Center
    Place of Publication: [Menlo Park, California]
    Additional Info: SLAC

Date

  • Creation: 2006-09-28

Language

  • English

Description

  • Content Description: The geometric and electronic structure of the active site of the non-heme iron enzyme nitrile hydratase (NHase) is studied using sulfur K-edge XAS and DFT calculations. Using thiolate (RS{sup -})-, sulfenate (RSO{sup -})-, and sulfinate (RSO{sub 2}{sup -})-ligated model complexes to provide benchmark spectral parameters, the results show that the S K-edge XAS is sensitive to the oxidation state of S-containing ligands and that the spectrum of the RSO- species changes upon protonation as the S-O bond is elongated (by {approx}0.1 {angstrom}). These signature features are used to identify the three cysteine residues coordinated to the low-spin Fe{sup III} in the active site of NHase as CysS{sup -}, CysSOH, and CysSO{sub 2}{sup -} both in the NO-bound inactive form and in the photolyzed active form. These results are correlated to geometry-optimized DFT calculations. The pre-edge region of the X-ray absorption spectrum is sensitive to the Z{sub eff} of the Fe and reveals that the Fe in [FeNO]{sup 6} NHase species has a Z{sub eff} very similar to that of its photolyzed Fe{sup III} counterpart. DFT calculations reveal that this results from the strong {pi} back-bonding into the {pi}* antibonding orbital of NO, which shifts significant charge from the formally t{sub 2}{sup 6} low-spin metal to the coordinated NO.

Subject

  • Keyword: Electronic Structure
  • Keyword: Iron Compounds
  • Keyword: X-Ray Spectroscopy
  • Keyword: Enzymes
  • Keyword: Other,Bio, Chem
  • Keyword: Absorption Spectroscopy
  • STI Subject Categories: 59 Basic Biological Sciences
  • Keyword: Molecular Structure
  • Keyword: Cysteine
  • Keyword: Density Functional Method Other,Bio, Chem
  • Keyword: Nitriles

Source

  • Journal Name: J.Am.Chem.Soc.128:533-541,2006

Collection

  • Name: Office of Scientific & Technical Information Technical Reports
    Code: OSTI

Institution

  • Name: UNT Libraries Government Documents Department
    Code: UNTGD

Resource Type

  • Article

Format

  • Text

Identifier

  • Report No.: SLAC-PUB-12101
  • Grant Number: AC02-76SF00515
  • Office of Scientific & Technical Information Report Number: 877206
  • Archival Resource Key: ark:/67531/metadc881144

Note

  • Display Note: http://www.slac.stanford.edu/cgi-wrap/pubpage?slac-pub-12101.html
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