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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Direct observation of a hydroperoxide surface intermediate upon visible light-driven water oxidation at an Ir oxide
Narayanappa Sivasankar1, Walter W Weare, Heinz Frei
1Physical Biosciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, California 94720, USA.
Abstract:
A surface hydroperoxide intermediate has been detected upon oxidation of water at an Ir oxide nanocluster catalyst system under pulsed excitation of a [Ru(bpy)(3)](2+) visible light sensitizer by recording of the OO vibrational mode at 830 cm(-1). Rapid-scan FT-IR spectroscopy of colloidal H(2)O, D(2)O, and D(2)(18)O solutions in the attenuated total reflection mode allowed spectral assignment of IrOOH on the basis of an observed D shift of 30 cm(-1), and (18)O shifts of 24 cm(-1) ((16)O(18)O) and 46 cm(-1) ((18)O(18)O). The laser pulse response of the infrared band is consistent with the kinetic relevancy of the intermediate. This is the first observation of a surface intermediate of oxygen evolution at an Ir oxide multielectron catalyst.
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