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Updated: Jun 12, 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
Recent applications of a synthetic model of cytochrome c oxidase: beyond functional modeling
James P Collman1, Somdatta Ghosh
1Department of Chemistry, Stanford University, Stanford, California 94305, USA. jpc@stanford.edu
Abstract:
This account reports recent developments of a functional model for the active site of cytochrome c oxidase (CcO). This CcO mimic not only performs the selective four-electron reduction of oxygen to water but also catalytically reduces oxygen using the biological one-electron reductant, cytochrome c. This functional model has been used to understand other biological reactions of CcO, for example, the interaction between the gaseous hormone, NO, and CcO. A mechanism for inactivating NO-CcO complexes is found to involve a reaction between oxygen and Cu(B). Moreover, NO is shown to be capable of protecting CcO from toxic inhibitors such as CN(-) and CO. Finally, this functional CcO model has been used to show how H(2)S could induce hibernation by reversibly inhibiting the oxygen binding step involved in respiration.
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