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Title: L-edge sum rule analysis on 3d transition metal sites: from d 10 to d 0 and towards application to extremely dilute metallo-enzymes

According to L-edge sum rules, the number of 3d vacancies at a transition metal site is directly proportional to the integrated intensity of the L-edge X-ray absorption spectrum (XAS) for the corresponding metal complex. In this study, the numbers of 3d holes are characterized quantitatively or semi-quantitatively for a series of manganese (Mn) and nickel (Ni) complexes, including the electron configurations 3d 10 → 3d 0. In addition, extremely dilute (<0.1% wt/wt) Ni enzymes were examined by two different approaches: (1) by using a high resolution superconducting tunnel junction X-ray detector to obtain XAS spectra with a very high signal-to-noise ratio, especially in the non-variant edge jump region; and (2) by adding an inert tracer to the sample that provides a prominent spectral feature to replace the weak edge jump for intensity normalization. In this publication, we present for the first time: (1) L-edge sum rule analysis for a series of Mn and Ni complexes that include electron configurations from an open shell 3d0 to a closed shell 3d 10; (2) a systematic analysis on the uncertainties, especially on that from the edge jump, which was missing in all previous reports; (3) a clearly-resolved edge jump between pre-L 3 andmore » post-L 2 regions from an extremely dilute sample; (4) an evaluation of an alternative normalization standard for L-edge sum rule analysis. XAS from two copper (Cu) proteins measured using a conventional semiconductor X-ray detector are also repeated as bridges between Ni complexes and dilute Ni enzymes. The differences between measuring 1% Cu enzymes and measuring <0.1% Ni enzymes are compared and discussed. As a result, this study extends L-edge sum rule analysis to virtually any 3d metal complex and any dilute biological samples that contain 3d metals.« less
Authors:
ORCiD logo [1] ; ORCiD logo [2] ; ORCiD logo [3] ; ORCiD logo [4] ; ORCiD logo [5] ; ORCiD logo [6] ; ORCiD logo [7]
  1. Univ. of California, Davis, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  2. Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
  3. Univ. of Hyogo, Tatsuno (Japan)
  4. Univ. of California, Davis, CA (United States)
  5. Univ. of Illinois, Urbana, IL (United States)
  6. Argonne National Lab. (ANL), Argonne, IL (United States)
  7. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Publication Date:
Report Number(s):
LLNL-JRNL-746682
Journal ID: ISSN 1463-9076; PPCPFQ; 142189
Grant/Contract Number:
AC02-06CH11357; AC52-07NA27344
Type:
Accepted Manuscript
Journal Name:
Physical Chemistry Chemical Physics. PCCP (Print)
Additional Journal Information:
Journal Name: Physical Chemistry Chemical Physics. PCCP (Print); Journal Volume: 20; Journal Issue: 12; Journal ID: ISSN 1463-9076
Publisher:
Royal Society of Chemistry
Research Org:
Argonne National Lab. (ANL), Argonne, IL (United States); Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
OSTI Identifier:
1434331
Alternate Identifier(s):
OSTI ID: 1465312

Wang, Hongxin, Friedrich, Stephan, Li, Lei, Mao, Ziliang, Ge, Pinghua, Balasubramanian, Mahalingam, and Patil, Daulat S. L-edge sum rule analysis on 3d transition metal sites: from d10 to d0 and towards application to extremely dilute metallo-enzymes. United States: N. p., Web. doi:10.1039/c7cp06624d.
Wang, Hongxin, Friedrich, Stephan, Li, Lei, Mao, Ziliang, Ge, Pinghua, Balasubramanian, Mahalingam, & Patil, Daulat S. L-edge sum rule analysis on 3d transition metal sites: from d10 to d0 and towards application to extremely dilute metallo-enzymes. United States. doi:10.1039/c7cp06624d.
Wang, Hongxin, Friedrich, Stephan, Li, Lei, Mao, Ziliang, Ge, Pinghua, Balasubramanian, Mahalingam, and Patil, Daulat S. 2018. "L-edge sum rule analysis on 3d transition metal sites: from d10 to d0 and towards application to extremely dilute metallo-enzymes". United States. doi:10.1039/c7cp06624d.
@article{osti_1434331,
title = {L-edge sum rule analysis on 3d transition metal sites: from d10 to d0 and towards application to extremely dilute metallo-enzymes},
author = {Wang, Hongxin and Friedrich, Stephan and Li, Lei and Mao, Ziliang and Ge, Pinghua and Balasubramanian, Mahalingam and Patil, Daulat S.},
abstractNote = {According to L-edge sum rules, the number of 3d vacancies at a transition metal site is directly proportional to the integrated intensity of the L-edge X-ray absorption spectrum (XAS) for the corresponding metal complex. In this study, the numbers of 3d holes are characterized quantitatively or semi-quantitatively for a series of manganese (Mn) and nickel (Ni) complexes, including the electron configurations 3d10 → 3d0. In addition, extremely dilute (<0.1% wt/wt) Ni enzymes were examined by two different approaches: (1) by using a high resolution superconducting tunnel junction X-ray detector to obtain XAS spectra with a very high signal-to-noise ratio, especially in the non-variant edge jump region; and (2) by adding an inert tracer to the sample that provides a prominent spectral feature to replace the weak edge jump for intensity normalization. In this publication, we present for the first time: (1) L-edge sum rule analysis for a series of Mn and Ni complexes that include electron configurations from an open shell 3d0 to a closed shell 3d10; (2) a systematic analysis on the uncertainties, especially on that from the edge jump, which was missing in all previous reports; (3) a clearly-resolved edge jump between pre-L3 and post-L2 regions from an extremely dilute sample; (4) an evaluation of an alternative normalization standard for L-edge sum rule analysis. XAS from two copper (Cu) proteins measured using a conventional semiconductor X-ray detector are also repeated as bridges between Ni complexes and dilute Ni enzymes. The differences between measuring 1% Cu enzymes and measuring <0.1% Ni enzymes are compared and discussed. As a result, this study extends L-edge sum rule analysis to virtually any 3d metal complex and any dilute biological samples that contain 3d metals.},
doi = {10.1039/c7cp06624d},
journal = {Physical Chemistry Chemical Physics. PCCP (Print)},
number = 12,
volume = 20,
place = {United States},
year = {2018},
month = {2}
}

Works referenced in this record:

Nickel hydrogenases: in search of the active site
journal, December 1994
  • Albracht, Simon P. J.
  • Biochimica et Biophysica Acta (BBA) - Bioenergetics, Vol. 1188, Issue 3, p. 167-204
  • DOI: 10.1016/0005-2728(94)90036-1