ライフサイエンスコーパス: flavin mononucleotide

1 s, including the analytically most demanding flavin mononucleotide.

2 r proteins that contain the prosthetic group flavin mononucleotide.

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

4 amine phosphate, thiamine pyrophosphate, and flavin mononucleotide.

5 ay crystal structure of EncD in complex with flavin mononucleotide.

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

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

8 n features an unprecedented binding site for flavin mononucleotide.

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

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

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

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

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

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

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

16 Flavin mononucleotide adenylyltransferase (FMNAT) cataly

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

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

19 t individuals with erythrocytes deficient in flavin mononucleotide and flavin adenine dinucleotide (F

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

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

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

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

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

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

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

27 rences in perfusate (eg, lactate, succinate, flavin mononucleotide) and tissues (eg, succinate, adeno

28 ox cofactors comprising seven Fe/S clusters, flavin mononucleotide, and a molybdenum ion coordinated

29 5 different subunits, a non-covalently bound flavin mononucleotide, and eight iron-sulfur clusters.

30 roperties of their chromophores (riboflavin, flavin mononucleotide, and flavin adenine dinucleotide)

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

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

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

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

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

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

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

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

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

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

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

42 Two flavin mononucleotide binding light, oxygen, or voltage

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

44 This correlated with loss of flavin mononucleotide binding.

45 0BM-3, a bacterial monooxygenase, contains a flavin mononucleotide-binding domain bearing a strong st

46 onal importance and suggested that the plant flavin mononucleotide-binding domain might be more flexi

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

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

49 Using flavin mononucleotide-binding proteins and glycosidases

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

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

52 , in tissues is dependent upon riboflavin as flavin mononucleotide, but whether this interaction is i

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

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

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

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

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

58 bial processes and depends on the prenylated flavin mononucleotide cofactor for catalysis.

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

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

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

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

63 yme, with each subunit covalently binding an flavin mononucleotide cofactor to a histidyl residue.

64 nes or aromatic compounds using a prenylated flavin mononucleotide cofactor.

65 sensing via flavin adenine dinucleotide and flavin mononucleotide cofactors have the same origin.

66 enzyme filament containing covalently bound flavin mononucleotide cofactors.

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

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

69 The flavodoxins are flavin mononucleotide-containing electron transferases.

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

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

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

73 The genes encoding flavin mononucleotide-containing oxidoreductases, design

74 Specifically, four different flavin mononucleotide-containing proteins were engineere

75 , while the formation of dead-end prenylated flavin mononucleotide cycloadducts occurs with distinct

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

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

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

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

80 coside and the liberated SQ is acted on by a flavin mononucleotide-dependent sulfoquinovose monooxyge

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

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

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

84 SNMP, reducing perfusate AST (p = 0.03) and flavin mononucleotide (FMN) (p = 0.01).

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

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

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

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

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

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

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

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

93 related, T-loop receptor motifs found in the flavin mononucleotide (FMN) and cobalamin (Cbl) riboswit

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

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

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

97 Flavin mononucleotide (FMN) and flavin adenine dinucleot

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

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

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

101 et3 did not show an MFE, but the addition of flavin mononucleotide (FMN) and simultaneous illuminatio

102 ith the known metabolic dependency of PLP on flavin mononucleotide (FMN) and suggest that riboflavin

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

104 Protein ligands of the flavin mononucleotide (FMN) and the plant-type [2Fe-2S]

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

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

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

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

109 The crystal structure reveals an flavin mononucleotide (FMN) binding site unique from all

110 fy covalently unpaired guanines critical for flavin mononucleotide (FMN) binding to the FMN riboswitc

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

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

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

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

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

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

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

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

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

120 By employing flavin mononucleotide (FMN) cofactor as a model system,

121 laments in solution, with a covalently bound flavin mononucleotide (FMN) cofactor at the interface be

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

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

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

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

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

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

128 and Thermoanaerobacter kivui employ a single flavin mononucleotide (FMN) cofactor to establish electr

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

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

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

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

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

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

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

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

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

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

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

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

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

142 3:1 between electrostatic plus van der Waals flavin mononucleotide (FMN) interdigitation and H-bondin

143 , namely the photo-induced transformation of flavin mononucleotide (FMN) into lumichrome, which incre

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

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

146 This study examined the predictive value of Flavin Mononucleotide (FMN) levels in the flush solution

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

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

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

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

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

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

153 The flavin mononucleotide (FMN) quinones in flavodoxin have

154 loited to generate a variety of (meta)stable flavin mononucleotide (FMN) radicals upon blue light abs

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

156 bsequent impaired mitochondrial function and Flavin Mononucleotide (FMN) release upon reperfusion.

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

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

159 we describe affinity-based profiling of the flavin mononucleotide (FMN) riboswitch to characterize l

160 the antibiotic Ribocil C, which targets the flavin mononucleotide (FMN) riboswitch, from a compound

161 Flavin mononucleotide (FMN) riboswitches are genetic ele

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

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

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

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

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

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

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

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

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

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

172 ailed study of the redox-active biomolecule, flavin mononucleotide (FMN), a molecule readily derived

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

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

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

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

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

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

179 forms flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), plays fundamental roles in

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

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

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

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

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

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

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

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

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

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

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

191 tase superfamily of enzymes encompasses many flavin mononucleotide (FMN)-dependent catalysts promotin

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

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

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

195 osphate (PLP)-dependent enzyme (Fub7), and a flavin mononucleotide (FMN)-dependent oxidase (Fub9) in

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

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

198 Flavin mononucleotide (FMN)-specific riboswitches, also

199 f unique gut microbial GUS enzymes that bind flavin mononucleotide (FMN).

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

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

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

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

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

205 c analysis of released mitochondrial flavin (flavin mononucleotide, FMN) in the machine perfusate.

206 oinduced electron transfer (ET) from reduced flavin mononucleotide (FMNH(-)) to nitrogen-containing s

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

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

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

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

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

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

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

214 5.0, 6.0, 7.0) containing a reduced form of flavin mononucleotide (FMNH2, 100 muM), a biogenic solub

215 3 kDa and containing two noncovalently bound flavin mononucleotides (FMNs).

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

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

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

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

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

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

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

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

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

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

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

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

228 nine dinucleotide as substrate to attach the flavin mononucleotide moiety to the target protein, anal

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

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

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

232 ing approach, proteins can be decorated with flavin mononucleotide or other flavins.

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

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

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

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

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

238 called arsH that encodes an NADPH-dependent flavin mononucleotide reductase.

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

240 An artificial flavin mononucleotide riboswitch and a randomly generate

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

242 internal ribosome entry site (IRES) and the flavin-mononucleotide riboswitch.

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

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

245 dulating complex I via interactions with the flavin mononucleotide site, proximal in the reaction pat

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

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

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

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

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

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

252 ovides time for cotranscriptional binding of flavin mononucleotide, which decreases the concentration