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L-Edge X-ray Magnetic Circular Dichroism of Ni Enzymes: Direct Probe of Ni Spin States
| Content Provider | Semantic Scholar |
|---|---|
| Author | Wang, Hongxin Patil, Daulat S. Ralston, Corie Y. Bryant, Craig William Cramer, Stephen P. |
| Copyright Year | 2001 |
| Abstract | Abstract X-ray magnetic circular dichroism (XMCD) measures the inner shell absorption difference between left and right circularly polarized X-rays in the presence of magnetic field, and provides us a direct probe of the spin values localized in the specific metal sites. In this study, using Desulfovibrio desulfuricans and Desulfovibrio gigas hydrogenases as examples, we have measured the L-edge XMCD of Ni enzymes for the first time and analyzed them in comparison with a doped high spin Ni II model complex. The reduced hydrogenases have a non-zero XMCD effect, which is consistent with a ‘high spin’ Ni II site. The magneto-optical sum rules have also been used to derive the orbital and spin angular momentum. |
| Starting Page | 865 |
| Ending Page | 871 |
| Page Count | 7 |
| File Format | PDF HTM / HTML |
| Volume Number | 114 |
| Alternate Webpage(s) | http://chemgroups.ucdavis.edu/~cramer/Publications_pdf/cramer_125.pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/S0368-2048%2800%2900375-3 |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
