Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope.
Clicks: 176
ID: 118516
2020
Article Quality & Performance Metrics
Overall Quality
Improving Quality
0.0
/100
Combines engagement data with AI-assessed academic quality
Reader Engagement
Emerging Content
0.6
/100
2 views
2 readers
Trending
AI Quality Assessment
Not analyzed
Abstract
Reductive dehalogenases are responsible for the reductive cleavage of carbon-halogen bonds during organohalide respiration. A variety of mechanisms have been proposed for these cobalamin and [4Fe-4S] containing enzymes, including organocobalt, radical, or cobalt-halide adduct based catalysis. The latter was proposed for the oxygen-tolerant cataboli reductive dehalogenase (NpRdhA). Here, we present the first substrate bound NpRdhA crystal structures, confirming a direct cobalt-halogen interaction is established and providing a rationale for substrate preference. Product formation is observed due to X-ray photoreduction. Protein engineering enables rational alteration of substrate preference, providing a future blue print for the application of this and related enzymes in bioremediation.Reference Key |
halliwell2020catabolicmicroorganisms
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
---|---|
Authors | Halliwell, Tom;Fisher, Karl;Payne, Karl A P;Rigby, Stephen E J;Leys, David; |
Journal | Microorganisms |
Year | 2020 |
DOI | E1344 |
URL | |
Keywords |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.