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Updated: May 18, 2026
![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
1H-ENDOR evidence for a hydrogen-bonding interaction that modulates the reactivity of a nonheme Fe(IV)═O unit
Muralidharan Shanmugam1, Genqiang Xue, Lawrence Que
1Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, USA.
Abstract:
We report that a novel use of 35 GHz (1)H-ENDOR spectroscopy establishes the presence in 1 of an Fe(IV)═O···H-O-Fe(III) hydrogen bond predicted by density functional theory computations to generate a six-membered-ring core for 1. The hydrogen bond rationalizes the difference in the C-H bond cleavage reactivity between 1 and 4(OCH(3)) (where a CH(3)O group has replaced the HO on the Fe(III) site). This result substantiates the seemingly paradoxical conclusion that the nonheme Fe(IV)═O unit of 1 not only has the electrophilic character required for H-atom abstraction but also retains sufficient nucleophilic character to accept a hydrogen bond from the Fe(III)-OH unit.
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