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The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: Implications for the enzyme mechanism

The active site electronic structure of the azide complex of substrate-bound human heme oxygenase-1, (hHO) has been investigated by (1)H NMR spectroscopy to shed light on the orbital/spin ground state as an indicator of the unique distal pocket environment of the enzyme. 2D (1)H NMR assignments of t...

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מידע ביבליוגרפי
Main Authors: Ogura, Hiroshi, Evans, John P., Peng, Dungeng, Satterlee, James D., de Montellano, Paul R. Ortiz, Mar, Gerd N. La
פורמט: Artigo
שפה:Inglês
יצא לאור: 2009
נושאים:
גישה מקוונת:https://ncbi.nlm.nih.gov/pmc/articles/PMC2676937/
https://ncbi.nlm.nih.gov/pubmed/19243105
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi802360g
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