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Mo K- and L-edge X-ray absorption spectroscopic study of the ADP·AlF_4^−-stabilized nitrogenase complex: comparison with MoFe protein in solution and single crystal

Corbett, Mary C. and Tezcan, F. Akif and Einsle, Oliver and Walton, Mika Y. and Rees, Douglas C. and Latimer, Matthew J. and Hedman, Britt and Hodgson, Keith O. (2005) Mo K- and L-edge X-ray absorption spectroscopic study of the ADP·AlF_4^−-stabilized nitrogenase complex: comparison with MoFe protein in solution and single crystal. Journal of Synchrotron Radiation, 12 (1). pp. 28-34. ISSN 0909-0495. https://resolver.caltech.edu/CaltechAUTHORS:20160913-092647561

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Abstract

The utility of using X-ray absorption spectroscopy (XAS) to study metalloproteins and, specifically, the enzyme complex nitrogenase, is highlighted by this study comparing both the structural and Mo-localized electronic features of the iron-molybdenum cofactor (FeMoco) in isolated MoFe protein and in the ADP·AlF_4^--stabilized complex of the MoFe protein with the Fe protein. No major differences are found at Mo between the two protein forms. The excellent quality of the data at both the Mo K and L edges will provide a baseline for analysis of other intermediates in the nitrogenase cycle. A new capability to delineate various contributions in the resting state of FeMoco is being pursued through polarized single-crystal XAS. The initial results point to the feasibility of using this technique for the analysis of scattering from the as yet unidentified atom at the center of FeMoco.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1107/S0909049504027827DOIArticle
http://scripts.iucr.org/cgi-bin/paper?S0909049504027827PublisherArticle
ORCID:
AuthorORCID
Tezcan, F. Akif0000-0002-4733-6500
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 2005 International Union of Crystallography. Received 23 February 2004; Accepted 22 October 2004. This work was supported by NIH grants RR-01209 (KOH) and GM45162 (DCR). The X-ray data were measured at SSRL, a national user facility operated by Stanford University on behalf of the US Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program and by the DOE, Office of Biological and Environmental Research.
Funders:
Funding AgencyGrant Number
NIHRR-01209
NIHGM45162
Department of Energy (DOE)UNSPECIFIED
Subject Keywords:nitrogenase; EXAFS; XAS; diffraction
Issue or Number:1
Record Number:CaltechAUTHORS:20160913-092647561
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160913-092647561
Official Citation:Corbett, M. C., Tezcan, F. A., Einsle, O., Walton, M. Y., Rees, D. C., Latimer, M. J., Hedman, B. & Hodgson, K. O. (2005). J. Synchrotron Rad. 12, 28-34.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:70299
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:21 Sep 2016 17:24
Last Modified:31 Jan 2020 22:37

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