ライフサイエンスコーパス: FMN

1 FMN diffuses through outer membrane porins where it acce

2 FMN hydrolases catalyze dephosphorylation of FMN to ribo

3 pproximately 46.1% FAD and approximately 45% FMN).

4 s for NADH and the primary electron acceptor FMN, and it provides a scaffold for seven iron-sulfur cl

5 ites for NADH, the primary electron acceptor FMN, and seven iron-sulfur clusters that form a pathway

6 ononucleotide (FMN) and glutamate to 8-amino-FMN via the intermediacy of 8-formyl-FMN.

7 formin Cappuccino (Capu) is conserved among FMN formins but distinct from other formins.

8 CpsUbiX: an FMN-bound wild type form and an FMN-unbound V47S mutant form.

9 ystal structures of two forms of CpsUbiX: an FMN-bound wild type form and an FMN-unbound V47S mutant

10 tic interactions of this triad can enable an FMN-NOSoxy interaction that is productive for electron t

11 ns showed that the At1g79790 gene encodes an FMN hydrolase (AtcpFHy1).

12 eishmaniasis, Leishmania major, expresses an FMN-containing nitroreductase (LmNTR) that metabolizes a

13 d via gene duplication and acquisition of an FMN-binding domain now prevalent in TyW1 of most eukaryo

14 ese findings reveal the first instance of an FMN-binding glycoside hydrolase and suggest a potential

15 TCBQ reductase (PcpD), an FMN- and NADH-dependent reductase, catalyzes the reducti

16 clic 4',5'-phosphate (cyclic FMN) through an FMN lyase domain.

17 erminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes.

18 es, displaying distinct sites for F420-0 and FMN ligands that partially overlap.

19 erminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 a

20 members within the Loop 1, mini-Loop 1, and FMN-binding classes of gut microbial GUS enzymes can rea

21 g exogenously acquired FAD, yielding AMP and FMN.

22 he C-terminal reductase domain binds FAD and FMN and the cosubstrate NADPH.

23 like mammalian NOS that contain both FAD and FMN binding domains within a single polypeptide chain, b

24 50 reductase (CPR) domain containing FAD and FMN cofactors in distinct domains of the CPR.

25 lectron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of

26 ming a salt bridge between the NADPH/FAD and FMN domains in the conformationally closed structure to

27 Both FAD and FMN flavin groups mediate the transfer of NADPH derived

28 restingly, significant reductions in FAD and FMN levels were observed before the onset of degeneratio

29 for electron transfer from NADPH via FAD and FMN to its redox partners.

30 om NADPH to cytochromes P450 via its FAD and FMN.

31 nthases (NOSs), which contain NADPH/FAD- and FMN-binding domains.

32 cking resulted in models of the NOS heme and FMN subdomain bound to calmodulin.

33 nel electron transfer of NfoR via Cu(II) and FMN.

34 tions that alternate between interflavin and FMN-heme electron transfer steps, structures of the holo

35 e observation that hydB contains NAD(P)+ and FMN binding sites, suggests that the hyd genes are speci

36 of direct coordination between substrate and FMN for productive catalysis.

37 chain provide greater stability to the anti-FMN conformation that leads to a right-handed FMN helix.

38 uria hominis, which confirmed that these are FMN binders.

39 al pi-pi alignment between the near-armchair FMN helix and the underlying nanotube lattice plays a cr

40 asing the extent of hydrogen bonding between FMN and a specific amino acid residue in the local prote

41 drolase and suggest a potential link between FMN and carbohydrate metabolism in the human gut microbi

42 w that they utilize a conserved site to bind FMN that is not essential for GUS activity, but can affe

43 he FMN-induced "turn-off" activities of both FMN riboswitches in Bacillus subtilis, allowing rib gene

44 demonstrate a tightly, non-covalently bound FMN in the active site of the enzyme.

45 ctron transfer to and from the tightly bound FMN.

46 Bacteria but not in Archaea is controlled by FMN-responsive riboswitches.

47 RbkR was stimulated by CTP and suppressed by FMN, a product of riboflavin kinase.

48 mes is unlike any structurally characterized FMN binders to date.

49 ntents of riboflavin and the flavo-coenzymes FMN and FAD.

50 lavin is a direct precursor of the cofactors FMN and FAD.

51 The bridging interaction appeared to control FMN subdomain interactions with both its electron donor

52 of riboflavin cyclic 4',5'-phosphate (cyclic FMN) through an FMN lyase domain.

53 Formation of the CYP17A1.FMN domain complex induced differential line broadening

54 6-S-cysteinyl flavin mononucleotide (6-S-Cys-FMN) as redox cofactors.

55 s for the plastid AtcpFHy1 and the cytosolic FMN hydrolase characterized previously.

56 As a consequence, our protein-encased FMN system produces O(2)(a(1)Delta(g)) with the uniquely

57 centrations of l-arginine (Arg), NADPH, FAD, FMN, tetrahydrobiopterin (BH4), and calmodulin, indicati

58 portant to experimentally determine the Fe...FMN distance to provide a key calibration for computatio

59 es the accessibility of oxygen to the flavin FMN chromophore and makes protein quenching less favoura

60 Bacterial dodecins bind the flavin FMN instead of riboflavin and exhibit a clearly differen

61 ucleotide (NADH) and a protein-bound flavin (FMN) cofactor.

62 d riboflavin and the cognate flavocoenzymes, FMN and FAD, by in vitro biotransformation with better t

63 Similarly, unusually weak XplA flavodoxin FMN binding (K(d) = 1.09 muM) necessitates its purificat

64 centers in the [Fe(III)][FMNH(*)] (FMNH(*): FMN semiquinone) form of a human inducible NOS (iNOS) bi

65 assist phosphate-C1' bond breakage following FMN reduction, leading to formation of the N5-C1' bond.

66 wed the domain-domain interaction needed for FMN reduction.

67 ating an additional proton transfer role for FMN in turnover of NO.

68 (II) and that Cys(163) is an active site for FMN binding.

69 Spir and formin (FMN)-type actin nucleators initiate actin polymerization

70 le of riboflavin and its two cofactor forms, FMN and FAD.

71 8-amino-FMN via the intermediacy of 8-formyl-FMN.

72 Free FMN and FAD were not detectable and only trace amounts o

73 es, albeit at no kinetic advantage over free FMN.

74 hanism to transfer reducing equivalents from FMN to the pterin substrate.

75 l medium) occurs when an electron moves from FMN(B) to riboflavin.

76 hat carries the electrons one at a time from FMN to a coenzyme Q molecule bound in the vicinity of th

77 suggest a pathway for electron transfer from FMN to heme and a mechanism for calmodulin activation of

78 cular, the pathway of electron transfer from FMN to heme, and the mechanism through which calmodulin

79 in movement, allowing electron transfer from FMN to the CYPOR redox partners.

80 d structural basis of electron transfer from FMN-hydroquinone to its partners, three deletion mutants

81 s increase with existing values for NAD(P)H4-FMN distances, based on charge-transfer complex absorban

82 MN conformation that leads to a right-handed FMN helix.

83 Human FMN cyclase, which splits FAD and other ribonucleoside d

84 es to further investigate how the changes in FMN domain conformational freedom impact the following:

85 pernatants, with a corresponding decrease in FMN and riboflavin.

86 atic SOD1 mice had a significant decrease in FMN survival compared with WT, which suggests an increas

87 ible alternative function of Acg proteins in FMN storage or sequestration from other biochemical path

88 and Tyr171 residues play important roles in FMN binding.

89 cterial physiology, covalently incorporating FMN cofactors into numerous respiratory enzymes that use

90 eptor pathway is involved in axotomy-induced FMN death in WT and is partially responsible for the mSO

91 pport the injured MN, leading to Fas-induced FMN death.

92 uropil surrounding the two different injured FMN populations contained distinct molecular differences

93 Regardless of their ultimate fate, injured FMNs respond with a vigorous pro-survival/regenerative m

94 Phosphatase activity of AtcpFHy1 is FMN-specific, as assayed with 19 potential substrates.

95 MtrC is significantly weaker than with known FMN-binding proteins, but identify a mildly preferred in

96 port, we describe the preparation of labeled FMN isotopologues enriched with (15)N and (13)C isotopes

97 evels of FMN are sufficient ("high levels"), FMN binding to FMN riboswitches leads to a reduction of

98 rs that form a pathway for electrons linking FMN to the terminal electron acceptor, ubiquinone, which

99 usters that form an electron pathway linking FMN to the terminal electron acceptor, ubiquinone, which

100 measured the reduction potential of the LovK FMN cofactor.

101 al-time optical measurement of mitochondrial FMN release in machine perfusates of livers disclosed a

102 Presymptomatic mSOD1(G93A) mouse facial MN (FMN) are more susceptible to axotomy-induced cell death

103 ossible role for this molecule in modulating FMN and FAD levels in the treponemal periplasm.

104 anella oneidensis and flavin mononucleotide (FMN in fully oxidized quinone form) using computational

105 ctive non-heme diiron/flavin mononucleotide (FMN) active site.

106 ) is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide, which are essentia

107 enzyme that converts flavin mononucleotide (FMN) and glutamate to 8-amino-FMN via the intermediacy o

108 rotein ligands of the flavin mononucleotide (FMN) and the plant-type [2Fe-2S] cluster of CntB and als

109 pathway and harbors a flavin mononucleotide (FMN) as a potential cofactor.

110 non-covalently bound flavin mononucleotide (FMN) as cofactor, acquires its native alpha/beta paralle

111 structure reveals an flavin mononucleotide (FMN) binding site unique from all other flavodoxins that

112 he environment of the flavin mononucleotide (FMN) chromophore; in iLOV, the methyl group of Thr-394 "

113 -2 requires a reduced flavin mononucleotide (FMN) coenzyme to carry out this redox neutral isomerizat

114 tein and/or intrinsic flavin mononucleotide (FMN) cofactor are isotopically labeled with (2)H, (15)N,

115 te site proximal to a flavin mononucleotide (FMN) cofactor.

116 turnover with NO are flavin mononucleotide (FMN) dependent, implicating an additional proton transfe

117 yl phosphate chain of flavin mononucleotide (FMN) induces a right-handed helix that enriches the left

118 ic plus van der Waals flavin mononucleotide (FMN) interdigitation and H-bonding interactions, respect

119 ced transformation of flavin mononucleotide (FMN) into lumichrome, which increases the accessibility

120 Flavin mononucleotide (FMN) is a coenzyme for numerous proteins involved in key

121 superfamily in which flavin mononucleotide (FMN) is firmly anchored to the protein.

122 two adjacently bound flavin mononucleotide (FMN) ligands, one deeply buried and tightly bound and on

123 -2S] cluster, and one flavin mononucleotide (FMN) per enzyme.

124 y a phosphate-bearing flavin mononucleotide (FMN) photocatalyst on high surface area metal-oxide film

125 de in the presence of flavin mononucleotide (FMN) resulted in the reversible formation of a stable fl

126 C, which targets the flavin mononucleotide (FMN) riboswitch, from a compound lacking whole-cell acti

127 Flavin mononucleotide (FMN) riboswitches are genetic elements, which in many ba

128 The IET from the flavin mononucleotide (FMN) to heme domains is essential in the delivery of ele

129 nal members of a rare flavin mononucleotide (FMN) variant class, and also variants of c-di-GMP-I and

130 ate, vitamin B12, and flavin mononucleotide (FMN) were measured for all subjects.

131 acceptor of electrons flavin mononucleotide (FMN), and a chain of seven iron-sulfur clusters that car

132 inucleotide (FAD) and flavin mononucleotide (FMN), are two key cofactors involved in oxidative metabo

133 luding riboflavin and flavin mononucleotide (FMN), into the surrounding medium to act as extracellula

134 inucleotide (FAD) and flavin mononucleotide (FMN), the physiologically relevant catalyst dephosphoryl

135 binds the chromophore flavin mononucleotide (FMN), we have developed a promising photosensitizer that

136 rization of UbiX as a flavin mononucleotide (FMN)-binding protein, no decarboxylase activity has been

137 rns out to be unusual flavin mononucleotide (FMN)-binding proteins that have probably arisen by gene

138 vidence indicated the flavin mononucleotide (FMN)-binding riboswitch aptamer adopted a 'bound-like' s

139 d the presence of one flavin mononucleotide (FMN)-binding site and two iron-sulfur cluster sites, con

140 enzyme (Fub7), and a flavin mononucleotide (FMN)-dependent oxidase (Fub9) in synthesizing the picoli

141 ion, and a paucity of flavin mononucleotide (FMN)-dependent proteins in these families.

142 f noncovalently bound flavin mononucleotide (FMN).

143 GUS enzymes that bind flavin mononucleotide (FMN).

144 mitochondrial flavin (flavin mononucleotide, FMN) in the machine perfusate.

145 of wild-type (WT) mouse facial motoneurons (FMNs) surviving with FMNs undergoing significant cell de

146 the mechanisms underlying the enhanced mSOD1 FMN loss after axotomy, we superimposed the facial nerve

147 T and is partially responsible for the mSOD1 FMN death.

148 ependent monooxygenase that requires an NADH:FMN oxidoreductase (EmoB) to provide FMNH2 as a cosubstr

149 Vibrio harveyi NADPH-FMN oxidoreductase (FRP) catalyzes flavin reduction by N

150 In this study, a new FMN hydrolase was purified by multistep chromatography a

151 hat is differentially expressed in the nitro-FMN reductase superfamily during redox cycling.

152 , constitute a new subclass within the nitro-FMN reductase superfamily.

153 hat is structurally reminiscent of the nitro-FMN reductase superfamily.

154 nds coded for enzymes belonging to the Nitro-FMN-reductase superfamily.

155 To generate nitric oxide (NO), the NOS FMN subdomain must interact with the NOSoxy domain to de

156 gages in a bridging interaction with the NOS FMN subdomain.

157 (2+)-dependent and proceeds with FAD but not FMN.

158 ripheral site could bind either the observed FMN (the electron donor for the overall reaction) or the

159 na flavodoxin, where the naturally occurring FMN cofactor is substituted by different analogs, makes

160 opted a 'bound-like' structure in absence of FMN, suggesting only local conformational changes upon l

161 and O(2)R activities upon simple addition of FMN.

162 phorylation of riboflavin and adenylation of FMN to produce FAD.

163 esulting enzyme catalyzes the adenylation of FMN with ATP to produce FAD and PP(i).

164 ere not detectable and only trace amounts of FMN were found in milk following acid treatment.

165 Overall, our results suggest that binding of FMN to MtrC is reversible and not highly specific, which

166 s, whereas Ser-390 anchors the side chain of FMN-interacting Gln-489 Our combined structural and muta

167 L was also found to catalyze cytidylation of FMN with CTP, making the modified FAD, flavin cytidine d

168 FMN hydrolases catalyze dephosphorylation of FMN to riboflavin.

169 the one-electron-reduced semiquinone form of FMN.

170 e oxidized and two-electron-reduced forms of FMN are detected.

171 led due to the oxidized and reduced forms of FMN-Na being stabilized by resonance structures.

172 The exact function of FMN in catalysis has not yet been clearly defined.

173 hydrogen bonds that the planar headgroup of FMN can form with this protein compared to FMN-binding p

174 onformationally more stable and incapable of FMN-to-heme ET.

175 We find that interaction of FMN with MtrC is significantly weaker than with known FM

176 type and no longer increased their level of FMN shielding in response to NADPH binding.

177 When cytoplasmic levels of FMN are sufficient ("high levels"), FMN binding to FMN r

178 ssion even in the presence of high levels of FMN.

179 fied complex I contained 0.94 +/- 0.1 mol of FMN, 29.0 +/- 0.37 mol of iron, and 1.99 +/- 0.07 mol of

180 assessment of the translational potential of FMN riboswitch binders against wild-type Gram-negative b

181 In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FM

182 variants, both in absence and in presence of FMN.

183 t time that ascertaining the binding rate of FMN as a function of ionic strength can be used as a too

184 mbrane binding of Spir to the recruitment of FMN, a pivotal step for initiating actin nucleation at v

185 C(1) catalyzes the reduction of FMN by NADH to provide FMNH(-) as a substrate for C(2).

186 ectron density for the isoalloxazine ring of FMN and induced a conformational change in residues of t

187 hin 20 angstrom of the isoalloxazine ring of FMN.

188 vironment, we decrease the susceptibility of FMN to undesired photoinitiated electron-transfer reacti

189 nteractions with the isoalloxazine system of FMN that are usually provided by protein side chains.

190 olved in or responsive to the interaction of FMNs and non-neuronal cells.

191 s cluster with genes for Na(+)-NQR and other FMN-binding flavoproteins in bacterial genomes and encod

192 ermolecular interactions with the overlaying FMN helix, impart enantioselection.

193 t 380 and 460 nm, characteristic of oxidized FMN.

194 uman inducible NOS (iNOS) bidomain oxygenase/FMN construct.

195 the dipole interactions between paramagnetic FMN and heme iron centers in the [Fe(III)][FMNH(*)] (FMN

196 sequence a previously identified plastidial FMN hydrolase AtcpFHy1 (At1g79790), belonging to the hal

197 highly modified flavin cofactor, prenylated FMN (prFMN).

198 utilizes the recently discovered prenylated FMN (prFMN) cofactor, and requires oxidative maturation

199 se enzyme that requires the novel prenylated FMN cofactor for activity.

200 ylase enzyme Fdc1 is dependent on prenylated FMN (prFMN), a recently discovered cofactor.

201 not catalyze the reverse reaction to produce FMN and ATP from FAD and PP(i).

202 Project database and identified 14 putative FMN-binding GUSs.

203 ther; the latter extends to one of the redox FMN cofactors.

204 d in other studies) suggest that the reduced FMN coenzyme of IDI-2 functions as an acid/base catalyst

205 ward the compact form protecting the reduced FMN cofactor from engaging in unspecific electron transf

206 redox states; (iv) reactivity of the reduced FMN domain toward cytochrome c; (v) response to calmodul

207 N, NADH, and flavin reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET

208 genic CYP17A1, the cytochrome P450 reductase FMN domain delivers both electrons, and b5 is an alloste

209 ring flavin derivatives, such as riboflavin, FMN, and FAD, as well as lumichrome, a photodegradation

210 tPyrP2 decreased accumulation of riboflavin, FMN, and FAD.

211 762N) of a conserved residue on the enzyme's FMN subdomain caused the NO synthesis activity to double

212 Higher serum FMN levels were significantly associated with increased

213 e reduced flavin in IDI-2 catalysis, several FMN analogues with altered electronic properties were ch

214 Axotomized presymptomatic SOD1 FMNs displayed a dynamic pro-survival/regenerative respo

215 reased susceptibility of presymptomatic SOD1 FMNs to axotomy-induced cell death and, by extrapolation

216 the assembly of the membrane-associated Spir.FMN complex.

217 ution experiment with chemically synthesized FMN-N5-oxide and (18)O2 labeling studies.

218 lyzes the RFK activity, while the N-terminal FMN-adenylyltransferase (FMNAT) exhibits the FMNAT activ

219 hain "flipping" of Leu-472, and the terminal FMN phosphate shows increased anchoring.

220 We found previously that FMN hydrolase activity in pea chloroplasts is Mg(2+)-dep

221 Recently, we showed that FMN-free diferrous FDP from Thermotoga maritima exposed

222 The FMN cofactor is not reduced by either NADH or NADPH, but

223 The FMN domain of one monomer was located close to the heme

224 The FMN domain outcompetes b5 for binding to CYP17A1 in the

225 The FMN-binding domain of UbiX is composed of three neighbor

226 ive hinge allows a best compromise among the FMN domain interactions and associated electron transfer

227 and (vi) the rates of interflavin ET and the FMN domain conformational dynamics.

228 nkage between a dimethylallyl moiety and the FMN N5 and C6.

229 different relative orientation, between the FMN domain and the bound CaM.

230 at hydrogen bonding interactions between the FMN N1, O2, and ribityl hydroxyls and the surrounding pr

231 tial input of two electrons delivered by the FMN domain of NADPH-cytochrome P450 reductase.

232 ate (PNP) oxidation to PLP, catalyzed by the FMN-dependent enzyme PNP oxidase (PNPOx).

233 During catalysis, the FMN subdomain cycles between interaction with an NADPH-F

234 ases (NOSs), two flexible hinges connect the FMN domain to the rest of the enzyme and may guide its i

235 chain of iron-sulfur clusters connecting the FMN of FdsB with the active-site molybdenum center of Fd

236 ational results reveal that constraining the FMN fluorophore yields improved photochemical properties

237 t here that the protein RibR counteracts the FMN-induced "turn-off" activities of both FMN riboswitch

238 OV, the methyl group of Thr-394 "crowds" the FMN isoalloxazine ring, Leu-470 triggers side chain "fli

239 through the FMN subdomain and diminished the FMN-to-heme electron transfer by 90%, whereas mutations

240 ct interactions between the heme domain, the FMN subdomain, and calmodulin were observed.

241 avin cofactor, but dithionite eliminated the FMN peaks, indicating successful electron transfer to MM

242 in the affinity of the R229W variant for the FMN cofactor.

243 isotope effect specifically arising from the FMN suggests that vibrations local to the active site pl

244 and thereby it facilitates the IET from the FMN to the catalytic heme site.

245 etween residues Asp(147) and Arg(514) in the FMN and FAD domains, respectively.

246 te the bridging interaction (Arg(752) in the FMN subdomain and Glu(47) in CaM).

247 s to gain access to electrons located in the FMN-domain are favored in the absence of bound coenzyme.

248 ansfer into FAD and then distribute into the FMN domain for further transfer to internal or external

249 eletion mutants in a conserved loop near the FMN were characterized.

250 ane structure, topology, and dynamics of the FMN binding domain of CYPOR in a native membrane-like en

251 proximity to the solvent-exposed edge of the FMN cofactor along with other residues distributed aroun

252 Chemical reduction of the FMN cofactor of LovK attenuates the light-dependent ATPa

253 can occur without redox participation of the FMN cofactor.

254 ow the spatial and temporal behaviors of the FMN domain impact catalysis by the NOS flavoprotein doma

255 Conformational freedom of the FMN domain is thought to be essential for the electron t

256 ngement and the CaM-dependent release of the FMN domain that coordinates to drive electron transfer a

257 omain, whereas in the open state, one of the FMN domains rotates away from its FAD domain and travers

258 Formin 2 (Fmn2), a member of the FMN family of formins, plays an important role in early

259 h the NAD pool, presumably the flavin of the FMN moiety (site I(F)) and the other dependent not only

260 spin P450, and the elevated potential of the FMN semiquinone/hydroquinone couple (-172 mV) is also an

261 roduction is an IET-competent complex of the FMN-binding domain and heme domain, and thereby it facil

262 nvoked a role for large scale motions of the FMN-binding domain in shuttling electrons from the FAD-b

263 d a conformational change in residues of the FMN-binding pocket that display peptide-bond flipping up

264 Third, binding and kinetic analysis of the FMN-binding site mutants of these five GUSs show that th

265 Structural comparison of the FMN-bound wild type form with the FMN-free form reveals

266 We investigated the role of the FMN-FAD/NADPH hinge in rat neuronal NOS (nNOS) by constr

267 tinamide ring stacks onto the re-face of the FMN.

268 uctase, and ferredoxin could also reduce the FMN peaks.

269 s Tyr-401 and Phe-485 in phiLOV sandwich the FMN isoalloxazine ring from both sides, whereas Ser-390

270 In the closed state, the FMN domain closely contacts the FAD domain, whereas in t

271 The right-handed twist that the FMN helix imposes to the underlying nanotube, similar to

272 tructural review of the PDB reveals that the FMN-binding site employed by these enzymes is unlike any

273 aM from increasing electron flux through the FMN subdomain and diminished the FMN-to-heme electron tr

274 dsB and Fe(2)S(2) in FdsG, are closer to the FMN than they are in other NADH dehydrogenases.

275 omposed of multiple domains, among which the FMN binding domain (FBD) is the direct electron donor to

276 stence of a second conformation in which the FMN domain is involved in a different interdomain interf

277 ion and a cross-monomer arrangement with the FMN domain rotated away from the NADPH-FAD center, towar

278 ough complementary charged residues with the FMN-binding site region of Ndor1 to perform electron tra

279 son of the FMN-bound wild type form with the FMN-free form reveals a significant conformational diffe

280 ariants reported here are located within the FMN lyase domain.

281 ion kinetics and had less shielding of their FMN subdomains compared with wild type and no longer inc

282 ing structural and functional data from this FMN-binding GUS, we analyzed the 279 unique GUS sequence

283 ed to the plant-type [2Fe-2S] cluster and to FMN in the form of a flavin semiquinone radical.

284 ze the transfer of the AMP portion of ATP to FMN to produce FAD and pyrophosphate (PP(i)).

285 e sufficient ("high levels"), FMN binding to FMN riboswitches leads to a reduction of rib gene expres

286 icrobe Faecalibacterium prausnitzii binds to FMN on a surface groove located 30 angstrom away from th

287 ns both free (3.3 A resolution) and bound to FMN (2.95 A resolution).

288 an electron moves from the 2Fe-2S center to FMN(C), while the translocation of sodium across the mem

289 f FMN can form with this protein compared to FMN-binding proteins.

290 s rapidly and almost completely converted to FMN by flavokinases.

291 lar extracts of S. oneidensis convert FAD to FMN, whereas extracts of ushA mutants do not, and fracti

292 nsfer electrons intramolecularly from FAD to FMN.

293 everal aspects of catalysis are sensitive to FMN-FAD/NADPH hinge length and that the native hinge all

294 mic space, where it is hydrolysed by UshA to FMN and adenosine monophosphate (AMP).

295 s may facilitate rapid intraflavin and trans FMN-to-heme electron transfers (ETs).

296 This produces two FMN conformations (syn and anti) analogous to DNA.

297 ependent flavin reductase family and can use FMN or FAD as a prosthetic group to catalyze reductive d

298 omplex is a dimer that covalently binds with FMN and Cu(II)-binding pocket is located at the interfac

299 use facial motoneurons (FMNs) surviving with FMNs undergoing significant cell death after axotomy.

300 otomy-induced cell death than wild-type (WT) FMN, which suggests additional CNS pathology.