| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152494 | Journal of Inorganic Biochemistry | 2017 | 30 Pages |
Abstract
New enhanced density functional calculations reveal that His195, strongly implicated in the mechanism of the enzyme nitrogenase, can undergo reversible proton transfers, dihydrogen bond formation, and H2 formation in its interactions with the active site FeMo-cofactor (FeMo-co).249
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Ian Dance,