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On the reaction mechanism of flavin-sensitized photoregulation of Monoraphidium braunii nitrate reductase by José A. Navarro; Mercedes Roncel; Miguel A. De la Rosa is a Medicine article available to read on EtoBox.

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Nitrate reductase from the green alga Mwwraphidium braunii is reversibly inactivated by reduction on irradiation in the presence of flavins and an electron donor; the process is markedly accelerated by cyanide anions. When the enzyme is depleted of its endogenous flavin adenine dinucleotide (FAD), a significant lag period of l-2 min is observed before photoinactivation takes place. This lag period is not observed if flavins (except FAD) are previously photoreduced in the reaction mixture; in this case the inactivation kinetics depend on the type of flavin used. The photoinactivation process is accompanied by reduction of the haem prosthetic groups. The flavin-sensitized photoinactivation of nitrate reductase is dependent on ionic strength; this appears to be due to complementary electrostatic interactions between the reduction site of the protein and the exogenous flavins. Flavins can also photosensitize the reactivation of the cyanide-inactivated reduced enzyme (either native or FAD-depleted nitrate reductase) in the absence of added electron donors. The mechanism of flavin-mediated nitrate reductase photoregulation is discussed.

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Author

José A. Navarro; Mercedes Roncel; Miguel A. De la Rosa

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1011-1344)

Published

1991

Language

EN

Field

Medicine (Physical Sciences)