Infrared spectroscopy provides insight into the role of dioxygen in the nitrosylation pathway of a [2Fe2S] cluster iron-sulfur protein.
We use infrared spectroscopy to demonstrate the critical role that trace O2 plays in determining the products formed when a [2Fe2S] cluster protein reacts with nitric oxide (NO). The observed importance of O2 may have physiological relevance, as many pathogens sense NO using iron-sulfur proteins and...
Main Authors: | Grabarczyk, D, Ash, P, Vincent, K |
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Format: | Journal article |
Sprog: | English |
Udgivet: |
American Chemical Society
2014
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