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Role of the Covalent and Noncovalent Flavins in Sarcosine Oxidase
Book chapter

Role of the Covalent and Noncovalent Flavins in Sarcosine Oxidase

Kalla Kvalnes-Krick and Marilyn Schuman Jorns
Chemistry and Biochemistry of Flavoenzymes, pp 425-436
1991
DOI: https://doi.org/10.1201/9781351070584-16

Abstract

Flavin Semiquinone Covalent Flavin Electron Transfer Flavoprotein Acyl CoA Dehydrogenase Phenol Hydroxylase Biradical Intermediate Heterocyclic Amines Adrenodoxin Reductase Room Temperature Electron Paramagnetic Resonance Sarcosine Dehydrogenase Trimethylamine Dehydrogenase Arthrobacter Ureafaciens Cyclohexanone Monooxygenase Sarcosine Oxidase American Chemical Society ETF Flavoprotein Oxidases Single Binding Site NADPH Cytochrome P-450 Reductase Steady State Kinetic Studies
The initial, half-reduced form of the enzyme is rapidly converted to a biradical form via comproportionation of the reduced noncovalent flavin with the oxidized covalent flavin. The stability of the sulfite complex formed with the covalent flavin in semiapoprotein was similar to that observed with native enzyme. The mechanism suggested for corynebacterial sarcosine oxidase is similar in many respects to the mechanism proposed for NADPH-cytochrome P-450 reductase which also contains two nonequivalent flavins and forms a biradical intermediate during catalysis. In addition to covalently bound flavin, the corynebacterial sarcosine oxidases and the enzyme from Arthrobacter ureafaciens contain noncovalently bound flavin. The data suggest that the corynebacterial enzymes will provide an interesting opportunity to study the mechanism of interflavin electron transfer. The noncovalent flavin in the corynebacterial enzymes has been identified as flavin adenine dinucleotide. The stability of the sulfite complex formed with the covalent flavin in semiapoprotein was similar to that observed with native enzyme.

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