Immobilized enzyme electron spin resonance

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Immobilized enzyme electron spin resonance (IE-ESR) is an electron spin resonance technique used to detect short lived radicals generated from enzyme reactions. This method is an alternative to the more commonly used continuous-flow or fast-flow ESR method.


The IE-ESR method was developed in the laboratory of Roanld P. Mason at the National Institute of Environmental Health Sciences/National Institutes of Health (NIEHS/NIH) by post doctoral fellows Bradley E. Sturgeon and Yeong-Renn Chen. The IE-ESR method was first used to detect the tyrosine iminoxyl radical.[1] This radical is the 1-electron oxidized form of nitrosotyrosine that was a results of the tyrosyl radical reacting with nitric oxide. A second publication using the IE-ESR method showed the increase in peroxidase activity of cytochrome c as a result of HOCl treatment.[2] The complete paper describing the method was published in 2003.[3]


  1. ^ J. Biol. Chem., 276(49), 45516-45521, 2001
  2. ^ J. Biol. Chem., 277(33), 29781-29791, 2002
  3. ^ Anal. Chem., 75(19), 5006-5011, 2003.