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First- and second-sphere contributions to Fe(II) site activation by cosubstrate binding in nonheme Fe enzymes

Nonheme Fe(II) enzymes exhibit a general mechanistic strategy where binding all cosubstrates opens a coordination site on the Fe(II) for O(2) activation. This study shows that strong-donor ligands, steric interactions with the substrate and second-sphere H-bonding to the facial triad carboxylate all...

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Библиографические подробности
Главные авторы: Light, Kenneth M., Hangasky, John A., Knapp, Michael J., Solomon, Edward I.
Формат: Artigo
Язык:Inglês
Опубликовано: 2014
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC3976902/
https://ncbi.nlm.nih.gov/pubmed/24292428
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c3dt53201a
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