ライフサイエンスコーパス: FMO

1 FMO consists of three monomers arranged in C3 symmetry w

2 FMO enzymes (FMOs) play a key role in the processes of d

3 FMO methodology was successfully used as part of a ratio

4 FMO mutants, on the other hand, produced both hemiketal

5 FMO needs NADPH as a cofactor in addition to the prosthe

6 FMO provides a large fraction of the oxidizing necessary

7 FMO theory and distortion/interaction energy control hav

8 FMO theory has been used to rationalize the lack of regi

9 FMOs are conserved in eukaryotes and induced by multiple

10 FMOs might reduce the risk of phospholipidosis of CAD-li

11 on enzyme flavin-containing monooxygenase-2 (FMO-2).

12 n-assisted process for better donor-acceptor FMO overlap, the third oxidized Cu center in the trinucl

13 As part of the human genome effort, an FMO-like gene, FMO6, was identified between FMO3 and FMO

14 ve enzyme with characteristics typical of an FMO isoform.

15 ges resulting from altering the 3'-end of an FMO were investigated with human FMO3.

16 DPH-binding sites, that are common to TR and FMO domains, abolishes all outputs.

17 nna-Matthews-Olson light-harvesting antenna (FMO) protein has been a model system for understanding p

18 s probably due to the degradation of the apo-FMO protein at different stages after it does not bind t

19 sulfur atoms, SAC and SBC, were much better FMO substrates than those having the less nucleophilic s

20 to hinge on a very sensitive balance between FMO interactions, electrostatics, and steric effects.

21 opriate type of red blood cell lysis buffer, FMO or isotype controls to identify rare cell population

22 ich is opposite to what would be expected by FMO considerations.

23 N-oxide and S-oxide metabolites produced by FMOs are often active metabolites.

24 ng the Fenna-Matthews-Olson antenna complex (FMO) as a model system, theoretical studies incorporatin

25 ,5-bis(phenylethynyl)benzene shows congruent FMOs.

26 n and also the implications of the decreased FMO/chlorosome stoichiometry are discussed in terms of t

27 iazine and exon 3- (exon 4 for FMO4) deleted FMOs were not able to catalyze the S- and N-oxygenation

28 or-acceptor substitution leads to a disjoint FMO pattern, while the parent 1,4-distyryl-2,5-bis(pheny

29 FMO enzymes (FMOs) play a key role in the processes of detoxification

30 rification and characterization of the first FMO protein variant generated via replacement of the est

31 sity is determined by the expression of five FMO genes, named FMO1 to FMO5, and their variants.

32 hers in the optical spectra calculations for FMO using ab initio site energies and excitonic coupling

33 A reduced slope (0.2-0.3) was found for FMO: this may be due to a different reaction mechanism i

34 However, in silico methods for FMO metabolism prediction are not yet available.

35 Here, we present an overview of evidence for FMOs' involvement in aging and disease, discussing the b

36 bilizing, there is a decrease in the forward FMO interaction that is offsetting.

37 cts on the regioselectivity are derived from FMO orbital interactions and the extent of electron tran

38 these transcripts would encode a functional FMO enzyme.

39 dies were done with two selective functional FMO substrates, methimazole, and 10-(N,N-dimethylaminope

40 Most identified FMO splice variants either caused a frame-shift or lacke

41 body of recent evidence, however, implicates FMOs in aging, several diseases, and metabolic pathways.

42 emperature, which never has been observed in FMO.

43 evidence that quantum coherence survives in FMO at physiological temperature for at least 300 fs, lo

44 ell as emission spectroscopy from individual FMO complexes at low temperatures.

45 The individual FMO complexes are subjected to very fast spectral fluctu

46 Intestinal FMO-2 is also activated by dietary restriction (DR) and

47 ontrol reactivity because, while the inverse FMO interaction becomes more stabilizing, there is a dec

48 enes encoding putative homologs of mammalian FMOs, K08C7.2, K08C7.5, Y39A1A.19, F53F4.5 and H24K24.5,

49 nzymes are related to those of the mammalian FMOs, which oxygenate nucleophilic substrates, YUC6 oxyg

50 the mutant cells contain a much less mature FMO protein.

51 vity of the flavin-containing monooxygenase (FMO) can be modulated by a number of nitrogen-containing

52 In humans, flavin-containing monooxygenase (FMO) functional diversity is determined by the expressio

53 The flavin-containing monooxygenase (FMO) gene family is conserved and ancient with represent

54 ase (ALDH), flavin-containing monooxygenase (FMO), and cytochrome P450 (CYP) enzymes.

55 a bacterial flavin-containing monooxygenase (FMO), is found widespread in marine bacteria and is resp

56 talyzed by a flavin-dependent monooxygenase (FMO) activity internal to the last module of the PKS.

57 one requires an FAD-dependent monooxygenase (FMO) PhnB, which catalyzes the C2 aromatic hydroxylation

58 s encoding flavin-containing monooxygenases (FMOs) 1 and 4 of man.

59 The flavin-containing monooxygenases (FMOs) are a family of five microsomal enzymes important

60 The flavin-containing monooxygenases (FMOs) are important for the oxidation of a variety of en

61 Flavin-containing monooxygenases (FMOs) are primarily studied as xenobiotic metabolizing e

62 Flavin-containing monooxygenases (FMOs) attach an oxygen atom to the insoluble nucleophili

63 UCCA (YUC) flavin-containing monooxygenases (FMOs) catalyze a rate-limiting step in auxin biosynthesi

64 scens) and flavin-containing monooxygenases (FMOs, from Schizosaccharomyces pombe and hog liver micro

65 and hepatic flavin-dependent monooxygenases (FMOs) efficiently oxidize TMA to TMAO.

66 onstitute a family of flavin monooxygenases (FMOs), with an important role in auxin (IAA) biosynthesi

67 cal, conserved YUCCA sequences: FATGY motif, FMO signature sequence, and FAD-binding and NADP-binding

68 l pi-pi* FMOs of C-C pi bonds or the pi-n(+) FMOs of heavier group 14 alkyne analogues.

69 cros component correlates with the amount of FMO protein in the isolated RCC complex.

70 is enzyme displayed other characteristics of FMO enzymes, with rapid depletion of enzyme activity upo

71 The locations and extents of labeling of FMO on the native membrane in comparison with it alone a

72 Here we analyze the functional mechanism of FMO from Schizosaccharomyces pombe using the crystal str

73 xenobiotic-metabolising enzymes, examples of FMOs exist that have evolved to metabolise specific endo

74 nal change in the oxidative half-reaction of FMOs.

75 he endogenous substrate(s) and regulation of FMOs.

76 rast, endogenous functions and substrates of FMOs are less well understood.

77 ic eigenstates for the Fenna-Matthews-Olson (FMO) antenna complex, which can be used to improve theor

78 e antenna complex, the Fenna-Matthews-Olson (FMO) antenna protein from green sulfur bacteria, complet

79 the membrane-attached Fenna-Matthews-Olson (FMO) antenna protein functions as a "wire" to connect th

80 their coupling in the Fenna-Matthews-Olson (FMO) bacteriochlorophyll complex, which is found in gree

81 energy transfer in the Fenna-Matthews-Olson (FMO) complex of photosynthetic green sulphur bacteria, h

82 t-protein complex, the Fenna-Matthews-Olson (FMO) complex, is suggestive that quantum coherence might

83 rred to the RC via the Fenna-Matthews-Olson (FMO) complex.

84 of the widely studied Fenna-Matthews-Olson (FMO) light-harvesting complex.

85 riochlorophyll) of the Fenna-Matthews-Olson (FMO) photosynthetic pigment protein complex.

86 ay of (3)Bchl a of the Fenna-Matthews-Olson (FMO) protein.

87 mmetric and asymmetric Fenna-Matthews-Olson (FMO) trimers, combined with absorption difference anisot

88 rption difference anisotropy measurements on FMO trimers from the green bacterium Chlorobium tepidum,

89 43 kcal/mol) and frontier molecular orbital (FMO) energy gaps.

90 d to the inverse frontier molecular orbital (FMO) interaction between the azadiene LUMO and alkene HO

91 d donor-acceptor frontier molecular orbital (FMO) overlap.

92 The fragment molecular orbital (FMO) quantum-mechanical (QM) method provides a complete

93 Frontier molecular orbital (FMO) theory is predicated in part on this concept.

94 edictions of the frontier molecular orbital (FMO) theory.

95 in an unoccupied frontier molecular orbital (FMO) with correct orientation and distal O character for

96 described by the frontier molecular-orbital (FMO) model.

97 e difference in frontier molecular orbitals (FMO) of the metal-oxo and substrate-oxo bonds.

98 Localization of frontier molecular orbitals (FMOs) along different axes of these cruciforms makes the

99 s elucidate key frontier molecular orbitals (FMOs) and their contribution to H atom abstraction react

100 n the important frontier molecular orbitals (FMOs) for this reaction, the unoccupied beta-spin d(xz/y

101 the calculated frontier molecular orbitals (FMOs) of Ar(iPr(4))GaGaAr(iPr(4)) are of pi-pi symmetry,

102 bstituents, the frontier molecular orbitals (FMOs) of these cruciforms are either congruent, i.e., HO

103 dox-active dpi* frontier molecular orbitals (FMOs).

104 g regions compared with those encoding other FMO isoforms.

105 imazole, a flavin-containing mono-oxygenase (FMO) substrate, inhibited S-oxidation of all four conjug

106 talyzed by flavin-containing mono-oxygenase (FMO; refs 7,8), and tissue localization and functional s

107 isotropy and oxo donor strength that perturb FMOs and affect reactivity.

108 reactions than permitted by the usual pi-pi* FMOs of C-C pi bonds or the pi-n(+) FMOs of heavier grou

109 tions along the same mechanistic pathway (pi-FMO pathway) with similar reactivity but also have an ad

110 onserved cysteine residue (Cys-85) preserves FMO but suppresses TR activity and stress tolerance, whe

111 fluorescence, and CD spectra of the purified FMO variant protein are similar to those of the wild-typ

112 Sequence analysis of this putative FMO family member revealed nothing that would a priori a

113 ated as substrates for cDNA-expressed rabbit FMO isoforms FMO1, FMO2, FMO3, and FMO5.

114 The spatially separated FMOs permit the independent manipulation of the HOMO and

115 e unoccupied alpha-spin d(z2) orbital (sigma-FMO pathway).

116 holipidosis of CAD-like drugs, although some FMOs metabolites seem to be neurotoxic and hepatotoxic.

117 e of approximately 20 s whereas that of some FMOs is >30 min.

118 ne derivatives with energetically stabilized FMOs.

119 ts validity for the case of the much-studied FMO dynamics as well as the canonical spin-boson model.

120 n simulations based on a threefold-symmetric FMO protein.

121 g the excitons within the Chlorobium tepidum FMO complex at 77 K.

122 o the transition state geometry, rather than FMO interactions or reaction thermodynamics, controls re

123 We find that FMO interactions do not control reactivity because, whil

124 = OMe, Me, CO 2Me, Cl, CN) and reveals that FMO interaction energies between the 1,3-dipole and the

125 These results show that FMO isoforms can catalyze cysteine conjugate S-oxidation

126 We propose that FMOs exist in the cell as a complex with a reduced form

127 Because these results suggested that FMOs were the major catalysts of SBC, SAC, and DCVC sulf

128 The FMO protein still assembles with the modified pigment, b

129 With the exception of FMO5, the FMO are encoded within a single gene cluster on human ch

130 spectra further reveals that "site 5" in the FMO complex plays a distinct role from other sites.

131 r two low-energy bacteriochlorophylls in the FMO protein from Chlorobaculum tepidum Removal of these

132 0/P840(+) from the decay of (3)Bchl a in the FMO protein.

133 Nonetheless, the FMO protein is able to quench energy transfer in aerobic

134 lectronic spectroscopy investigations of the FMO bacteriochlorophyll complex, and obtain direct evide

135 that probes solvent-exposed surfaces of the FMO by labeling solvent-exposed aspartic and glutamic ac

136 stem, we find that when certain sites of the FMO complex are subject to either the suppression of int

137 able one to calculate the Hamiltonian of the FMO complex in the site basis by fitting to the experime

138 al peaks in the 2D rephasing spectrum of the FMO complex obscure all but one of the crosspeaks at 77

139 duced, local defects or modifications of the FMO complex, and allows access to both the local and glo

140 e previously reported for this member of the FMO family of man.

141 efforts to characterize this isoform of the FMO gene family.

142 rolled to a great extent by two areas of the FMO primary structure (residues 381-432 and 433-465).

143 The assembly of the FMO protein and also the implications of the decreased F

144 ) and give information on the packing of the FMO protein in its native environment.

145 The smaller amount of the FMO protein in the mutant cell is probably due to the de

146 architecture for in vivo interactions of the FMO protein, the CM, and the chlorosome, ensuring highly

147 peptides show that the Bchl a #3 side of the FMO trimer interacts with the CM, which is consistent wi

148 ccessible by single-molecule techniques, the FMO complex exhibits ergodic behaviour.

149 siological temperature, and suggest that the FMO complex may work as a rectifier for unidirectional e

150 e instead of an epoxide, indicating that the FMO is involved in epoxidation rather than Baeyer-Villig

151 ial and temporal dynamics of EET through the FMO complex at physiological temperature are investigate

152 ed by the chlorosome is funneled through the FMO to the RC.

153 ductase activity (TR) that overlaps with the FMO domain involved in IAA biosynthesis.

154 The FMOs are more active than cytochromes in the brain and w

155 l for FMO3, the most relevant isoform of the FMOs in humans.

156 These studies experimentally probe the FMOs involved in the reactivity of FeIV=O (S = 1) model

157 Our results indicate that the FMOs and band gaps of benzobisoxazoles can be readily mo

158 It is not clear whether these FMO splice variants can oxygenate other substrates, incl

159 We apply the NNM to the entire trimeric FMO complex and find evidence for the existence of nonli

160 The differential contribution of the two FMOs to chlorination versus hydroxylation selectivity in

161 rotein are similar to those of the wild-type FMO protein except the conformations of most pigments ar

162 All previous studies have utilized wild-type FMO proteins from several species.

163 The structure of the wild-type FMO revealed that the prosthetic group FAD is an integra

164 model to a series of compounds with unknown FMO metabolism is also reported.

165 The variant FMO protein is less thermally stable than the wild type.

166 The excited-state lifetime of the variant FMO protein is unchanged from that of the wild type and