| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7754439 | Journal of Inorganic Biochemistry | 2017 | 7 Pages |
Abstract
We have revisited the crystal structures of [NiFe]-hydrogenase from desulfovibrio vulgaris Miyazaki in the several oxidized and reduced conditions. The NiâFe active site of the enzyme was partially damaged with Ni-elimination and formation of a disulfide bond by two cysteinyl ligands to the depleted Ni upon exposure to O2.504
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Koji Nishikawa, Satoko Mochida, Takeshi Hiromoto, Naoki Shibata, Yoshiki Higuchi,
![First Page Preview: Ni-elimination from the active site of the standard [NiFe]âhydrogenase upon oxidation by O2 Ni-elimination from the active site of the standard [NiFe]âhydrogenase upon oxidation by O2](/preview/png/7754439.png)