Loading...
|
Please use this identifier to cite or link to this item:
http://ir.ncue.edu.tw/ir/handle/987654321/15146
|
| Title: | Nickel Oxidation States of F430 Cofactor in Methyl-Coenzyme M Reductase |
| Authors: | Craft, Jennifer L.;Horng, Yih-Chern;Ragsdale, Stephen W.;Brunold, Thomas C. |
| Contributors: | 化學系 |
| Date: | 2004
|
| Issue Date: | 2013-01-07T02:15:49Z
|
| Publisher: | American Chemical Society |
| Abstract: | Magnetic circular dichroism (MCD) spectroscopy and variable-temperature variable-field MCD are used in combination with density functional theory (DFT) and time-dependent DFT (TD-DFT) calculations to characterize the so-called ox1-silent, red1, and ox1 forms of the Ni-containing cofactor F430 in methyl-coenzyme M reductase (MCR). Previous studies concluded that the ox1 state, which is the precursor of the key reactive red1 state of MCR, is a Ni(I) species that derives from one-electron reduction of the Ni(II)-containing ox1-silent state. However, our absorption and MCD data provide compelling evidence that ox1 is actually a Ni(II) species. In support of this proposal, our DFT and TD-DFT calculations indicate that addition of an electron to the ox1-silent state leads to formation of a hydrocorphin anion radical rather than a Ni(I) center. These results and biochemical evidence suggest that ox1 is more oxidized than red1, which prompted us to test a new model for ox1 in which the ox1-silent species is oxidized by one electron to form a thiyl radical derived from coenzyme M that couples antiferromagnetically to the Ni(II) ion. This alternative ox1 model, formally corresponding to a Ni(III)/thiolate resonance form but with predicted S = 1/2 EPR parameters reminiscent of a Ni(I) (3dx2−y2)1 species, rationalizes the requirement for reduction of ox1 to yield the red1 species and the seemingly incongruent EPR and electronic spectra of the ox1 state. |
| Relation: | J. Am. Chem. Soc., 126(13): 4068-4069 |
| Appears in Collections: | [化學系] 期刊論文
|
Files in This Item:
| File |
Size | Format | |
|---|
| index.html | 0Kb | HTML | 581 | View/Open |
|
All items in NCUEIR are protected by copyright, with all rights reserved.
|
