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 FMN is positioned asymmetrically within the junctional s

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

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

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

7 notable effects of mutations in the adjacent FMN domain on the heme structure in a human iNOS bidomai

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

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

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

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

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

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

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

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

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

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 g exogenously acquired FAD, yielding AMP and FMN.

21 ely pre-folded tertiary RNA architecture and FMN recognition mediated by conformational transitions w

22 ond between the backbone amide of Asn537 and FMN N5, the anionic ionization state of the hydroquinone

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

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

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 contains a flavin reductase domain (FAD and FMN) and a catalytic heme oxygenase domain (P450-type he

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

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

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

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 Dihydroorotate dehydrogenases (DHODs) are FMN-containing enzymes that catalyze the conversion of d

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 bond and/or salt-bridge interactions between FMN and Arg-229 and Ser-175.

42 the semiquinone/hydroquinone couple of both FMN and FAD are altered to a larger extent than the oxid

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 of the isoalloxazine ring of an enzyme-bound FMN prosthetic group as a hydride, and an active site ba

46 ctron transfer to and from the tightly bound FMN.

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

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

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

53 6-S-cysteinyl flavin mononucleotide (6-S-Cys-FMN) as redox cofactors.

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

55 ins clearly indicates that a properly docked FMN domain contributes to the observed L-Arg perturbatio

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

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

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

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

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

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

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

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

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

68 8-amino-FMN via the intermediacy of 8-formyl-FMN.

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

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

71 s electron transfer from FAD to FMN and from FMN to heme by adjusting the relative orientation and di

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

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

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

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

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

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

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

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

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

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

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

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

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

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

86 and Tyr171 residues play important roles in FMN binding.

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

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

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

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

91 Emerging evidence suggests that interdomain FMN-heme interactions are important in the formation of

92 tations and provided molecular insights into FMN-based control of gene expression in normal and ribof

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

94 on spectrum of CPR with that of the isolated FMN domain permitted identification of residues in the F

95 s a unique autoinhibitory insert (AI) in its FMN subdomain that represses nNOS reductase activities a

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

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

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

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

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

101 measured the reduction potential of the LovK FMN cofactor.

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

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

110 i luciferase bound to flavin mononucleotide (FMN) at 2.3 A.

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

112 -2 requires a reduced flavin mononucleotide (FMN) coenzyme to carry out this redox neutral isomerizat

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

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

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

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

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

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

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

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

121 -2S] cluster, and one flavin mononucleotide (FMN) per enzyme.

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

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

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

125 The flavin mononucleotide (FMN) serves as the one-electron donor to the heme iron,

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

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

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

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

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

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

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

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

134 n is a complex of the flavin mononucleotide (FMN)-binding domain and the heme domain, and thereby it

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

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

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

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

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

140 f noncovalently bound flavin mononucleotide (FMN).

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

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

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

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

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

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

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

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

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

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

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

152 (2+)-dependent and proceeds with FAD but not FMN.

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

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

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

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

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

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

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

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

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

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

163 FMN hydrolases catalyze dephosphorylation of FMN to riboflavin.

164 ractive target for structure-based design of FMN-like antimicrobial compounds.

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

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

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

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

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

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

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

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

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

174 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

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

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

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

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

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

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

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

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

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

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

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

186 structure in a human iNOS bidomain oxygenase/FMN construct have been observed by using low-temperatur

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

202 762N) of a conserved residue on the enzyme's FMN subdomain caused the NO synthesis activity to double

203 Higher serum FMN levels were significantly associated with increased

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

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

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

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

208 (FMN-shielded) and one common unbound state (FMN-deshielded).

209 hich it exists in two distinct bound states (FMN-shielded) and one common unbound state (FMN-deshield

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

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

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

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

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

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

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

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

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

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

220 We have co-expressed CaM and the FMN domain of human iNOS, which includes the CaM-binding

221 hows that the substitution of Arg-229 at the FMN binding site has led to a loss of hydrogen-bond and/

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

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

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

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

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

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

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

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

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

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

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

233 t that separates it from FAD and exposes the FMN, allowing it to interact with its redox partners.

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

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

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

237 s the interdomain electron transfer from the FMN to the catalytic heme site.

238 pivoting on the C terminus of the hinge, the FMN domain of the enzyme undergoes a structural rearrang

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

240 d that the conserved surface residues in the FMN domain (E546 and E603) play key roles in facilitatin

241 this study, we identify glutamate 658 in the FMN domain of human iNOS to be a critical residue for iN

242 permitted identification of residues in the FMN domain whose environment differs in the two situatio

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

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

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

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

247 n facilitating a productive alignment of the FMN and heme domains in iNOS.

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

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

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

251 can occur without redox participation of the FMN cofactor.

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

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

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

255 state because they guide the docking of the FMN domain to the heme domain.

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

257 egulate the conformational equilibria of the FMN module in rat neuronal NOS (nNOS).

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

259 cantly influence the redox properties of the FMN or the accumulation of the anionic semiquinone.

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

261 (iii) CaM destabilizes interaction of the FMN subdomain with the NADPH-FAD subdomain but does not

262 quilibrium model for the conformation of the FMN subdomain, in which it exists in two distinct bound

263 xidized and hydroquinone redox states of the FMN, none of the replacements studied significantly alte

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

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

266 The inherent plasticity of the FMN-binding pocket and the availability of large opening

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

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

269 ii) CaM binding has no direct effects on the FMN subdomain.

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

271 of mammalian cytochrome P450 reductase, the FMN semiquinone state is not thermodynamically stable an

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

273 We studied how each partner subdomain, the FMN redox state, and CaM binding may regulate the confor

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

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

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

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

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

279 n and provides several interactions with the FMN isoalloxazine ring, was targeted in this study.

280 a far greater capacity to interact with the FMN subdomain than does the oxygenase domain.

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

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

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

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

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

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

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

290 and regulates electron transfer from FAD to FMN and from FMN to heme by adjusting the relative orien

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 hydride transfer from both NADPH and NADH to FMN in the reductive half-reaction of pentaerythritol te

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

295 ed here: suppression of electron transfer to FMN and control of the conformational equilibrium of the

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

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

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

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.