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Determination by X-ray Absorption Spectroscopy of the Fe—Fe Separation in the Oxidized Form of the Hydroxylase of Methane Monooxygenase Alone and in the Presence of MMOD.
- Source :
-
Inorganic Chemistry . 7/26/2004, Vol. 43 Issue 15, p4579-4589. 11p. 2 Diagrams, 5 Charts, 13 Graphs. - Publication Year :
- 2004
-
Abstract
- The diiron active site in the hydroxylase of Methylococcus capsulatus (Bath) methane monooxygenase (MMOH) has been studied in the oxidized form by X-ray absorption spectroscopy (XAS). Previous investigations by XAS and X-ray crystallography have identified two different distances (3.0 and 3.4 Å) between the two Fe atoms in the dinuclear site. The present study has employed a systematic extended X-ray absorption fine structure (EXAFS) fitting methodology, utilizing known and simulated active site and relevant model structures, to determine unambiguously the Fe-Fe separation in the oxidized form of MMOH. Consistent and unique fits were only possible for an Fe-Fe distance of 3.0 Å. This methodology was then applied to study potential changes in the active site local structure in the presence of MMOD, a protein of unknown function in multi-component MMO. Fe K-edge and EXAFS analyses revealed negligible changes in the diiron site electronic and geometric structure upon addition of MMOD to oxidized MMOH. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00201669
- Volume :
- 43
- Issue :
- 15
- Database :
- Academic Search Index
- Journal :
- Inorganic Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 14133395
- Full Text :
- https://doi.org/10.1021/ic049716b