Spectrophotometric studies on lysine monooxygenase, a flavoprotein.
نویسندگان
چکیده
The spectral changes of the enzyme-hound FAD were investigated in the anaerobic and aerobic reactions of lysine monooxygenase, a flavoprotein. Under anaerobic conditions, the enzyme FAD was fully reduced with lysine via a transient intermediate having a broad absorption band in the long wavelength region. This anaerobic species was presumably involved in the dehydrogenation of lysine leading to the formation of an a-keto acid. During the steady state of the aerobic reaction, a separate spectral species with a long wavelength absorption was observed. Both lysine and oxygen were required for its appearance. Kinetic evidence supports the intermediacy of this species in the oxygenation of lysine to an acid amide.
منابع مشابه
The Structure of the Antibiotic Deactivating, N-hydroxylating Rifampicin Monooxygenase.
Rifampicin monooxygenase (RIFMO) catalyzes the N-hydroxylation of the natural product antibiotic rifampicin (RIF) to 2'-N-hydroxy-4-oxo-rifampicin, a metabolite with much lower antimicrobial activity. RIFMO shares moderate sequence similarity with well characterized flavoprotein monooxygenases, but the protein has not been isolated and characterized at the molecular level. Herein, we report cry...
متن کاملForm Follows Function: Structural and Catalytic Variation in the Class A Flavoprotein Monooxygenases
Flavoprotein monooxygenases (FPMOs) exhibit an array of mechanistic solutions to a common chemical objective; the monooxygenation of a target substrate. Each FPMO efficiently couples reduction of a flavin cofactor by NAD(P)H to oxygenation of the target substrate via a (hydro)peroxyflavin intermediate. This purpose of this review is to describe in detail the Class A flavoprotein hydroxylases (F...
متن کاملStyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system.
Two-component flavoprotein monooxygenases are emerging biocatalysts that generally consist of a monooxygenase and a reductase component. Here we show that Rhodococcus opacus 1CP encodes a multifunctional enantioselective flavoprotein monooxygenase system composed of a single styrene monooxygenase (SMO) (StyA1) and another styrene monooxygenase fused to an NADH-flavin oxidoreductase (StyA2B). St...
متن کاملBiochemical and Mechanistic Studies of Nitronate Monooxygenase and Roles of Histidine Residues in Select Flavoprotein Oxidases
Nitronate monooxygenase (NMO) catalyzes the flavin-dependent oxidation of propionate 3-nitronate (P3N) via the formation of an anionic flavosemiquinone. The oxidation of substrate includes the formation of a peroxy-nitro acid intermediate. P3N is activated to its radical form via a single electron transfer onto the FMN cofactor forming the anionic flavosemiquinone. Reoxidation of FMN cofactor f...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie
دوره 27 9 شماره
صفحات -
تاریخ انتشار 1972