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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
Electron paramagnetic resonance analyses of biotransformation reactions with cytochrome P-450 immobilized on
Martha Rosales-Hernández1, Lowell Kispert, Eduardo Torres-Ramírez
1Sección de Estudios de Posgrado e Investigación y Departamento de Bioquímica de la, Escuela Superior de Medicina del Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Mexico, D.F., Mexico.
Abstract:
Mobil Crystalline Material (MCM-41) can be used for the immobilization of enzymes and the investigation of electron transfer in biological systems. Electron transfer between MCM-41 with aluminum (Al-MCM-41) and cytochrome P-450 (CYP2B4) was observed using electron paramagnetic resonance (EPR). When CYP2B4 was immobilized by adsorption, it catalyzed the conversion of aniline to p-aminophenol. The electron transfer was evidenced when the signal with a g value (also called g-factor or spectroscopic manifestation of the magnetic moment) of 1.98 increased at the same time that the signal with a g value 2.24 decreased due to the addition of NADPH to CYP2B4 immobilized on Al-MCM-41, indicating that FeIII was reduced to FeII. Therefore, it is possible that Al-MCM-41 participates in the electron transfer process in biological systems.
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