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Title: Manganese L-edge X-ray absorption spectroscopy of manganese catalase from Lactobacillus plantarum and mixed valence manganese complexes

Abstract

The first Mn L-edge absorption spectra of a Mn metalloprotein are presented in this paper. Both reduced and superoxidized Mn catalase have been examined by fluorescence-detected soft X-ray absorption spectroscopy, and their Mn L-edge spectra are dramatically different. The spectrum of reduced Mn(II)Mn(II) catalase has been interpreted by ligand field atomic multiplet calculations and by comparison to model compound spectra. The analysis finds a 10 Dq value of nearly 1.1 eV, consistent with coordination by predominately nitrogen and oxygen donor ligands. For interpretation of mixed valence Mn spectra, an empirical simulation procedure based on the addition of homovalent model compound spectra has been developed and was tested on a variety of Mn complexes and superoxidized Mn catalase. This routine was also used to determine the oxidation state composition of the Mn in [Ba{sub 8}Na{sub 2}ClMn{sub 16}(OH){sub 8}(CO{sub 3}){sub 4}L{sub 8}] .53 H{sub 2}O (L=1,3-diamino-2-hydroxypropane-N,N,N`N`-tetraacetic acid). 27 refs., 6 figs.

Authors:
; ;  [1]
  1. Univ. of California, Davis, CA (United States) [and others
Publication Date:
OSTI Identifier:
199398
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of the American Chemical Society; Journal Volume: 118; Journal Issue: 1; Other Information: PBD: 10 Jan 1996
Country of Publication:
United States
Language:
English
Subject:
40 CHEMISTRY; MANGANESE COMPLEXES; ABSORPTION SPECTRA; ENZYMES; PROTEINS; ORGANOMETALLIC COMPOUNDS; X-RAY SPECTROSCOPY; ELECTRONIC STRUCTURE

Citation Formats

Grush, M.M., Chen, J., and George, S.J.. Manganese L-edge X-ray absorption spectroscopy of manganese catalase from Lactobacillus plantarum and mixed valence manganese complexes. United States: N. p., 1996. Web. doi:10.1021/ja951614k.
Grush, M.M., Chen, J., & George, S.J.. Manganese L-edge X-ray absorption spectroscopy of manganese catalase from Lactobacillus plantarum and mixed valence manganese complexes. United States. doi:10.1021/ja951614k.
Grush, M.M., Chen, J., and George, S.J.. Wed . "Manganese L-edge X-ray absorption spectroscopy of manganese catalase from Lactobacillus plantarum and mixed valence manganese complexes". United States. doi:10.1021/ja951614k.
@article{osti_199398,
title = {Manganese L-edge X-ray absorption spectroscopy of manganese catalase from Lactobacillus plantarum and mixed valence manganese complexes},
author = {Grush, M.M. and Chen, J. and George, S.J.},
abstractNote = {The first Mn L-edge absorption spectra of a Mn metalloprotein are presented in this paper. Both reduced and superoxidized Mn catalase have been examined by fluorescence-detected soft X-ray absorption spectroscopy, and their Mn L-edge spectra are dramatically different. The spectrum of reduced Mn(II)Mn(II) catalase has been interpreted by ligand field atomic multiplet calculations and by comparison to model compound spectra. The analysis finds a 10 Dq value of nearly 1.1 eV, consistent with coordination by predominately nitrogen and oxygen donor ligands. For interpretation of mixed valence Mn spectra, an empirical simulation procedure based on the addition of homovalent model compound spectra has been developed and was tested on a variety of Mn complexes and superoxidized Mn catalase. This routine was also used to determine the oxidation state composition of the Mn in [Ba{sub 8}Na{sub 2}ClMn{sub 16}(OH){sub 8}(CO{sub 3}){sub 4}L{sub 8}] .53 H{sub 2}O (L=1,3-diamino-2-hydroxypropane-N,N,N`N`-tetraacetic acid). 27 refs., 6 figs.},
doi = {10.1021/ja951614k},
journal = {Journal of the American Chemical Society},
number = 1,
volume = 118,
place = {United States},
year = {Wed Jan 10 00:00:00 EST 1996},
month = {Wed Jan 10 00:00:00 EST 1996}
}