ライフサイエンスコーパス: flavin mononucleotide

1 eous electrolyte based on the sodium salt of flavin mononucleotide.

2 pic agent to enhance the water solubility of flavin mononucleotide.

3 r proteins that contain the prosthetic group flavin mononucleotide.

4 NADP+ on inhibitor binding was mediated via flavin mononucleotide.

5 amine phosphate, thiamine pyrophosphate, and flavin mononucleotide.

6 n features an unprecedented binding site for flavin mononucleotide.

7 sitizers: anthraquinone-2,6-disulphonate and flavin mononucleotide.

8 folding coupled to binding of its cofactor, flavin mononucleotide.

9 r amine oxidases, this enzyme contains haem, flavin mononucleotide, 2Fe-2S and tetrahydrofolic acid c

10 r cluster ([4Fe-4S](2+)) and a 6-S-cysteinyl flavin mononucleotide (6-S-Cys-FMN) as redox cofactors.

11 Here we show that the flavin mononucleotide, a common redox cofactor, wraps ar

12 Recombinant NPH1 noncovalently binds flavin mononucleotide, a likely chromophore for light-de

13 y reporting potential-induced changes in the flavin mononucleotide active site of a flavoenzyme.

14 Flavin mononucleotide adenylyltransferase (FMNAT) cataly

15 The hydrophilic matrix arm comprises flavin mononucleotide and 8 iron-sulfur clusters involve

16 nine redox cofactors: a noncovalently bound flavin mononucleotide and eight iron-sulfur clusters.

17 ons through its conversion to coenzyme forms flavin mononucleotide and flavin adenine dinucleotide.

18 2)) is the precursor of the flavin coenzymes flavin mononucleotide and flavin adenine dinucleotide.

19 g ROS production in the mitochondria include flavin mononucleotide and flavin mononucleotide-binding

20 oxygen, or voltage (LOV) domains, which bind flavin mononucleotide and form a covalent adduct between

21 The photosensor YtvA binds flavin mononucleotide and regulates the general stress r

22 gh concentric pi-pi interactions between the flavin mononucleotide and the underlying graphene wall.

23 R VOLTAGE (LOV) domain binds the chromophore flavin mononucleotide and undergoes light-induced photoc

24 5 different subunits, a non-covalently bound flavin mononucleotide, and eight iron-sulfur clusters.

25 The homotetrameric enzyme required NADPH, flavin mononucleotide, and Mg(2+) for activity; K(m)(IPP

26 NADPH, flavin mononucleotide, and Mg2+ are required cofactors.

27 he enzyme readily hydrolyzed 5'-nucleotides, flavin mononucleotide, and O-phospho-L-Tyr.

28 amer complexes with adenosine monophosphate, flavin mononucleotide, arginine/citrulline and tobramyci

29 oreceptor kinase that binds two molecules of flavin mononucleotide as its chromophores and undergoes

30 The significantly higher affinity of the flavin mononucleotide assembly for (8,6)-single-walled c

31 In the presence of a surfactant, the flavin mononucleotide assembly is disrupted and replaced

32 The strength of the helical flavin mononucleotide assembly is strongly dependent on

33 sequence change (R116Q), predicted to affect flavin mononucleotide binding and binding of the two PNP

34 n enzyme intermediate and, together with the flavin mononucleotide binding cradle, we propose a novel

35 We have defined a novel flavin mononucleotide binding cradle, which is a recurre

36 Two flavin mononucleotide binding light, oxygen, or voltage

37 uding the conserved CGGHGY motif, a putative flavin mononucleotide binding site.

38 This correlated with loss of flavin mononucleotide binding.

39 0BM-3, a bacterial monooxygenase, contains a flavin mononucleotide-binding domain bearing a strong st

40 tochondria include flavin mononucleotide and flavin mononucleotide-binding domain of complex I, ubise

41 primary auxin-response gene that codes for a flavin mononucleotide-binding flavodoxin-like quinone re

42 Using flavin mononucleotide-binding proteins and glycosidases

43 sis reveals that FQR1 belongs to a family of flavin mononucleotide-binding quinone reductases.

44 unusually tight binding pocket accommodates flavin mononucleotide but not NAD(P)H.

45 of the Per-Arnt-Sim (PAS) family, contains a flavin mononucleotide chromophore that forms a covalent

46 adduct between a conserved cysteine and the flavin mononucleotide chromophore upon photoexcitation.

47 ntal constraints, derived from enzymatic and flavin mononucleotide cleavage, improve the accuracy of

48 d fragmentation and contraction of the bound flavin mononucleotide cofactor and cleavage of the ribit

49 lly neutral 5'-phosphate binding loop of the flavin mononucleotide cofactor binding site found in all

50 a ping-pong type mechanism, catalyzed by the flavin mononucleotide cofactor in the active site for NA

51 describe the thermodynamic properties of the flavin mononucleotide cofactor of Enterobacter cloacae n

52 tochrome and acidic residues surrounding the flavin mononucleotide cofactor of the flavodoxin.

53 -encoded proteins, iron-sulfur clusters, and flavin mononucleotide cofactor require the participation

54 containing two 4Fe-4S clusters and two FMN (flavin mononucleotide) cofactors.

55 ively, than that for the naturally occurring flavin mononucleotide complex.

56 The flavodoxins are flavin mononucleotide-containing electron transferases.

57 lldD and of other prokaryotic and eukaryotic flavin mononucleotide-containing enzymes that catalyze t

58 ic module was expressed in soluble form as a flavin mononucleotide-containing flavoprotein.

59 A monomeric, flavin mononucleotide-containing NG reductase was purifi

60 The genes encoding flavin mononucleotide-containing oxidoreductases, design

61 ith similarities to the aldolase class 1 and flavin mononucleotide dependent oxidoreductase and phosp

62 DH) from Pseudomonas putida, a member of the flavin mononucleotide-dependent alpha-hydroxy acid oxida

63 ase from Pseudomonas putida, a member of the flavin mononucleotide-dependent alpha-hydroxy acid oxida

64 al relationships of the functionally diverse flavin mononucleotide-dependent nitroreductase (NTR) sup

65 negative charge on the isoalloxazine ring of flavin mononucleotide during hydride transfer, as has be

66 found that an aliphatic (dodecyl) analog of flavin mononucleotide, FC12, leads to high dispersion of

67 tochrome MtrC from Shewanella oneidensis and flavin mononucleotide (FMN in fully oxidized quinone for

68 FDPs contain a distinctive non-heme diiron/flavin mononucleotide (FMN) active site.

69 se proteins by generating a covalent protein-flavin mononucleotide (FMN) adduct within sensory Per-AR

70 In addition, this enzyme complex houses one flavin mononucleotide (FMN) and 7-8 iron-sulfur clusters

71 FprA contains flavin mononucleotide (FMN) and a non-heme diiron site.

72 dioxygenase reductase (PDR), which contains flavin mononucleotide (FMN) and a plant-like ferredoxin

73 monomer, and a reductase (PDR) that contains flavin mononucleotide (FMN) and a plant-type ferredoxin

74 ltage-regulated (LOV1 and LOV2) domains bind flavin mononucleotide (FMN) and activate the phototropis

75 The complex between flavin mononucleotide (FMN) and apo-flavodoxin is domina

76 to cellular metabolism through formation of flavin mononucleotide (FMN) and flavin adenine dinucleot

77 OS C termini interrupt electron flux between flavin mononucleotide (FMN) and flavin adenine dinucleot

78 Riboflavin (vitamin B2) is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleot

79 n of a flavin-dependent enzyme that converts flavin mononucleotide (FMN) and glutamate to 8-amino-FMN

80 tio of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) and is functionally analogou

81 chanism has been proposed for the binding of flavin mononucleotide (FMN) and riboflavin to the apofla

82 ation of the initial interaction between the flavin mononucleotide (FMN) and the apoflavodoxin and th

83 biquinone biosynthesis pathway and harbors a flavin mononucleotide (FMN) as a potential cofactor.

84 doxin, which contains a non-covalently bound flavin mononucleotide (FMN) as cofactor, acquires its na

85 structure of V. harveyi luciferase bound to flavin mononucleotide (FMN) at 2.3 A.

86 Circular dichroism studies indicated that flavin mononucleotide (FMN) binding led to considerable

87 regions of prokaryotic mRNAs that encode for flavin mononucleotide (FMN) biosynthesis and transport p

88 ved the solution structure of the complex of flavin mononucleotide (FMN) bound to the conserved inter

89 usion TftC used NADH to reduce either FAD or flavin mononucleotide (FMN) but did not use NADPH or rib

90 n is known to involve formation of a triplet flavin mononucleotide (FMN) chromophore followed by the

91 OV2 cysteine residue and an internally bound flavin mononucleotide (FMN) chromophore.

92 nduced constraints in the environment of the flavin mononucleotide (FMN) chromophore; in iLOV, the me

93 Surprisingly, IDI-2 requires a reduced flavin mononucleotide (FMN) coenzyme to carry out this r

94 ual hydrogen bond acceptor with the N(3)H of flavin mononucleotide (FMN) cofactor and the amide hydro

95 e (PETNR) where the protein and/or intrinsic flavin mononucleotide (FMN) cofactor are isotopically la

96 oth redox couples of the noncovalently bound flavin mononucleotide (FMN) cofactor in the flavodoxin a

97 eijerinckii flavodoxin, the reduction of the flavin mononucleotide (FMN) cofactor is accompanied by a

98 nd covalent attachment of an analogue of the flavin mononucleotide (FMN) cofactor onto carboxylic fun

99 ctions using the isoalloxazine moiety of the flavin mononucleotide (FMN) cofactor stacked between two

100 eractions with the isoalloxazine ring of the flavin mononucleotide (FMN) cofactor that contribute to

101 two redox couples of the noncovalently bound flavin mononucleotide (FMN) cofactor through the differe

102 plex between NADPH and oxidized enzyme-bound flavin mononucleotide (FMN) cofactor, followed by rate-l

103 cans flavodoxin, which noncovalently binds a flavin mononucleotide (FMN) cofactor.

104 a type II' turn upon reduction of the bound flavin mononucleotide (FMN) cofactor.

105 ) acidic flavoprotein that contains a single flavin mononucleotide (FMN) cofactor.

106 iquinone/hydroquinone couple (Esq/hq) of the flavin mononucleotide (FMN) cofactor.

107 onheme diiron-carboxylate site proximal to a flavin mononucleotide (FMN) cofactor.

108 o and immediately after turnover with NO are flavin mononucleotide (FMN) dependent, implicating an ad

109 The redox potential of the flavin mononucleotide (FMN) hydroquinones for one-electr

110 ow that a 35mer RNA aptamer for the cofactor flavin mononucleotide (FMN) identified by in vitro evolu

111 study the electronic properties of oxidized flavin mononucleotide (FMN) in old yellow enzyme (OYE) a

112 oli led to a large increase in the amount of flavin mononucleotide (FMN) in the E. coli cell extract.

113 that the chiral D-ribityl phosphate chain of flavin mononucleotide (FMN) induces a right-handed helix

114 ff fluorescence signal, which corresponds to flavin mononucleotide (FMN) interconverting between the

115 3:1 between electrostatic plus van der Waals flavin mononucleotide (FMN) interdigitation and H-bondin

116 Flavin mononucleotide (FMN) is a coenzyme for numerous p

117 longs to the flavodoxin superfamily in which flavin mononucleotide (FMN) is firmly anchored to the pr

118 its an active site with two adjacently bound flavin mononucleotide (FMN) ligands, one deeply buried a

119 n, an electron-transfer protein containing a flavin mononucleotide (FMN) molecule as its prosthetic g

120 MTH538 also did not bind flavin mononucleotide (FMN) or coenzyme F(420).

121 2) as reductant; NmoB was similar to an NADH:flavin mononucleotide (FMN) oxidoreductase.

122 er, one plant-type [2Fe-2S] cluster, and one flavin mononucleotide (FMN) per enzyme.

123 aromatic hydrocarbons by a phosphate-bearing flavin mononucleotide (FMN) photocatalyst on high surfac

124 The flavin mononucleotide (FMN) quinones in flavodoxin have

125 uinone/hydroquinone couples of the protein's flavin mononucleotide (FMN) redox cofactor.

126 cleavage of the disulfide in the presence of flavin mononucleotide (FMN) resulted in the reversible f

127 bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangeme

128 Flavin mononucleotide (FMN) riboswitches are genetic ele

129 The flavin mononucleotide (FMN) serves as the one-electron d

130 After reconstitution with iron, sulfide, and flavin mononucleotide (FMN) the homologs contained six t

131 The IET from the flavin mononucleotide (FMN) to heme domains is essential

132 ein interdomain electron transfer (IET) from flavin mononucleotide (FMN) to heme is essential in nitr

133 it intraprotein electron transfer (IET) from flavin mononucleotide (FMN) to heme is essential in nitr

134 his amino acid, additional members of a rare flavin mononucleotide (FMN) variant class, and also vari

135 d amplified on the basis of its affinity for flavin mononucleotide (FMN) was covalently bound to the

136 al phosphate (PLP), folate, vitamin B12, and flavin mononucleotide (FMN) were measured for all subjec

137 e activity capable of reducing either FAD or flavin mononucleotide (FMN) with NADH as the reductant.

138 dies indicated that phototropin uses a bound flavin mononucleotide (FMN) within its light-oxygen-volt

139 for NADH, the primary acceptor of electrons flavin mononucleotide (FMN), and a chain of seven iron-s

140 ctors, flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), are two key cofactors invol

141 -bound cofactors: cytochrome P450-type heme, flavin mononucleotide (FMN), flavin adenine dinucleotide

142 entrations flavins, including riboflavin and flavin mononucleotide (FMN), into the surrounding medium

143 cted in cell extracts of bacterium BNC1 when flavin mononucleotide (FMN), NADH, and O2 were present.

144 ne, heme, flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), or NADPH.

145 and that residue T236, the binding site for flavin mononucleotide (FMN), resides in the cytoplasm.

146 actors flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), the physiologically relevan

147 NADH is oxidized by a noncovalently bound flavin mononucleotide (FMN), then seven iron-sulfur clus

148 to a LOV2 protein that binds the chromophore flavin mononucleotide (FMN), we have developed a promisi

149 state for NO production is a complex of the flavin mononucleotide (FMN)-binding domain and the heme

150 re we report the preparation of the isolated flavin mononucleotide (FMN)-binding domain of nNOS with

151 nd biochemical characterization of UbiX as a flavin mononucleotide (FMN)-binding protein, no decarbox

152 The Acg family turns out to be unusual flavin mononucleotide (FMN)-binding proteins that have p

153 Prior evidence indicated the flavin mononucleotide (FMN)-binding riboswitch aptamer a

154 rmatic analysis revealed the presence of one flavin mononucleotide (FMN)-binding site and two iron-su

155 these associated negative regulators by its flavin mononucleotide (FMN)-containing light-oxygen-volt

156 thylallyl diphosphate isomerase (IDI-2) is a flavin mononucleotide (FMN)-dependent enzyme that cataly

157 drogenase (MDH) from Pseudomonas putida is a flavin mononucleotide (FMN)-dependent enzyme that oxidiz

158 n suggests that BluB is a member of the NADH/flavin mononucleotide (FMN)-dependent nitroreductase fam

159 , most of unknown function, and a paucity of flavin mononucleotide (FMN)-dependent proteins in these

160 A flavin mononucleotide (FMN)-dependent riboswitch from th

161 Flavin mononucleotide (FMN)-specific riboswitches, also

162 unction as binding sites for the chromophore flavin mononucleotide (FMN).

163 The latter contains a known binding site for flavin mononucleotide (FMN).

164 ontained one molecule of noncovalently bound flavin mononucleotide (FMN).

165 n kinase domain and two structurally similar flavin-mononucleotide (FMN) binding domains designated L

166 His-tagged Fre reduced flavins (flavin mononucleotide [FMN] and flavin adenine dinucleot

167 A direct transfer of the reduced flavin mononucleotide (FMNH(2)) cofactor of Vibrio harve

168 found to have decreased affinity for reduced flavin mononucleotide (FMNH(2)).

169 ononucleotide (Kd, 7 micrometers) or reduced flavin mononucleotide (FMNH2) (Kd < 10(-8) M) per 90,200

170 NEET specifically interacts with the reduced flavin mononucleotide (FMNH2) and that FMNH2 can quickly

171 similar to a monooxygenase that uses reduced flavin mononucleotide (FMNH2) as reductant; NmoB was sim

172 The reduced flavin mononucleotide (FMNH2) generated by FRP must be s

173 this loop are governed by binding of either flavin mononucleotide (FMNH2) or polyvalent anions.

174 5.0, 6.0, 7.0) containing a reduced form of flavin mononucleotide (FMNH2, 100 muM), a biogenic solub

175 3 kDa and containing two noncovalently bound flavin mononucleotides (FMNs).

176 rmed when the nucleotide and the active-site flavin mononucleotide have complementary oxidation state

177 gated the redox reaction kinetics of reduced flavin mononucleotide (i.e., FMNH(2)) and reduced ribofl

178 Alternatively, NADH oxidation, by the flavin mononucleotide in complex I, can be coupled to th

179 er from nicotinamide adenine dinucleotide to flavin mononucleotide in morphinone reductase proceeds v

180 domain, a specialized PAS domain that binds flavin mononucleotide in plant phototropins, we show tha

181 ccurred for residues near the surface of the flavin mononucleotide, including 87-90 (loop 1), and for

182 lic domain; it comprises NADH oxidation by a flavin mononucleotide, intramolecular electron transfer

183 n aerobic organisms, and its requirement for flavin mononucleotide is even more uncommon in catalysis

184 During catalysis, NADH oxidation by a flavin mononucleotide is followed by electron transfer t

185 The primary electron acceptor, flavin-mononucleotide, is within electron transfer dista

186 This enzyme binds one flavin mononucleotide (Kd, 7 micrometers) or reduced fla

187 dox domains modulate ROS production from the flavin mononucleotide moiety and iron-sulfur clusters.

188 dynamic light scattering and to contain one flavin mononucleotide molecule per monomer.

189 A redox flow battery using flavin mononucleotide negative and ferrocyanide positive

190 Bacterially expressed LOV domains bind flavin mononucleotide noncovalently and are photochemica

191 n PNPO affected residues involved in binding flavin mononucleotide or pyridoxal 5'-phosphate and many

192 ted aliphatic acids and utilize a prenylated flavin mononucleotide (prFMN) as cofactor, bound adjacen

193 sing a newly identified cofactor, prenylated flavin mononucleotide (prFMN).

194 opt an alpha+beta fold and together bind two flavin mononucleotide prosthetic groups at the dimer int

195 Flavins (riboflavin and flavin mononucleotide) recently have been shown to be ex

196 ract with electron shuttle molecules such as flavin mononucleotide, resulting in the formation of hig

197 An artificial flavin mononucleotide riboswitch and a randomly generate

198 Using experimental data for flavin mononucleotide riboswitch as a guide, we show tha

199 monella enterica serovar Typhimurium and the flavin mononucleotide-sensing ribB riboswitch from Esche

200 cence lifetime measurements of the intrinsic flavin mononucleotide show marked differences between "l

201 by opcA inactivation, but rather the reduced flavin mononucleotide substrate of luciferase is limitin

202 share key interactions involving their bound flavin mononucleotide that suggest a unique catalytic be

203 It contains a flavin mononucleotide to oxidize NADH, and an unusually

204 It contains a flavin mononucleotide to oxidize NADH, and eight iron-su

205 We use a biological cofactor, flavin mononucleotide, to demonstrate the power of synch

206 tinct synthetic mimic of the natural ligand, flavin mononucleotide, to repress riboswitch-mediated ri