ライフサイエンスコーパス: FADH2

1 l as the ultimate acceptor of electrons from FADH2.

2 lavin reductase that uses NAD(P)H to produce FADH2.

3 iquinone radical and, finally, fully reduced FADH2.

4 he binary VioA.FADH2 and of the ternary VioA.FADH2.2-(1H-indol-3-ylmethyl)prop-2-enoic acid complex w

5 ergy transfer observed for enzyme containing FADH2 and [6S]-, [6R]-, or [6R,S]-5,10-CH+-H4folate (the

6 s of reducing power and energy such as NADH, FADH2 and ATP, respectively, reflecting the fact that th

7 Structures of the binary VioA.FADH2 and of the ternary VioA.FADH2.2-(1H-indol-3-ylmeth

8 alf-reaction of MurB, namely, reoxidation of FADH2 and reduction of the enolpyruvyl substrate.

9 does not use dioxygen to re-oxidize reduced FADH2 and thus does not produce hydrogen peroxide; inste

10 nzymes typically depend on either NAD(P)H or FADH2 as hydride source for reduction purposes.

11 yield observed for folate in the absence of FADH2, as expected for Forster-type energy transfer.

12 The reaction of FADH2, Cl-, and O2 in the active site generates the powe

13 iate (t1/2 = 63 h at 4 degrees C) when RebH, FADH2, Cl-, and O2 react in the absence of substrate try

14 electron donor, a dinucleotide mimic of the FADH2 cofactor containing O at the 5'-end and 2'-deoxyad

15 d for the NADH (mitochondrial complex I) and FADH2 (complex II) pathways in both the resting and maxi

16 e oxidation-reduction potentials for the FAD/FADH2 couple (n = 2) were also comparable to the wild-ty

17 rmination of the redox potential for the FAD/FADH2 couple yields a value of -118 mV; the protein envi

18 pA is a reduced flavin adenine dinucleotide (FADH2)-dependent monooxygenase that converts 2,4,6-TCP t

19 Surprisingly, the FADH2-dependent halogenase PltA catalyzes chlorination a

20 in reductase and halogenase components of an FADH2-dependent halogenase, a class of enzymes involved

21 , we identify KtzQ and KtzR as tandem acting FADH2-dependent halogenases that work sequentially on fr

22 f quenching by flavin radical (EQ = 0.96) or FADH2 (EQ = 0.89) is the same for both folate isomers.

23 thered to the enzyme EncM and converted into FADH2 (Fl(red)) during substrate turnover.

24 and TcpA demonstrated that TcpX(H) provided FADH2 for TcpA catalysis.

25 e NADH-dependent reduction of FAD to provide FADH2 for the halogenase.

26 flavin cofactor in the two-electron reduced FADH2 form.

27 rbance band beyond 900 nm attributable to an FADH2-->NAD+ charge transfer interaction is generated du

28 The second FADH2, in contrast, transfers its electrons to the singl

29 In contrast, energy transfer from folate to FADH2 is sensitive to the stereochemical configuration a

30 d mitochondria were energised using NADH- or FADH2-linked substrates.

31 (-1)) forming tight, dimeric, and air-stable FADH2-NAD(P) charge-transfer complexes ineffective in el

32 ive rise to the formation of a very stable E-FADH2.NAD+ complex.

33 led an asymmetric mechanism in which the two FADH2.NAD+ per reduced dimer display kinetic inequivalen

34 nt for intramolecular electron transfer from FADH2 of the active site at RuIII, k(intra), equals 4.4

35 phorylation capacity for the succinate-using FADH2 pathway remained intact (2.6+/-0.3 versus 2.4+/-0.

36 ns lead to differential behavior as only one FADH2 per dimer binds NAD+ tightly to give the charge-tr

37 further support the conclusion that the two FADH2 per dimer in wild-type enzyme can be described as

38 ng light energy to the fully reduced flavin (FADH2) reaction center at high efficiency (EET = 0.92).

39 analogy with monooxygenases, we predict that FADH2 reacts with O2 to make peroxyflavin, which is deco

40 In PdR, the flavin adenine dinucleotide (FAD/FADH2) redox center acts as a transformer by accepting t

41 ells slowly generate electron equivalents as FADH2 through beta-oxidation of saturated fatty acids, w

42 t chain by shuttling elections from NADH and FADH2 to coenzyme Q (CoQ) and cytochrome c.

43 o succinate is coupled with the oxidation of FADH2 to FAD.

44 ced by NADPH, but electrons cannot flow from FADH2 to the mixed disulfide bond.

45 e propose a model for the electron flow from FADH2, to the 4Fe-4S clusters, to the heme, and finally

46 that a reduced flavin adenine dinucleotide (FADH2)-utilizing monooxygenase converted 2,4,6-TCP to 6-

47 dicated that tcpA, tcpB, and tcpC encoded an FADH2-utilizing monooxygenase, a probable flavin reducta

48 g primers designed from conserved regions of FADH2-utilizing monooxygenases and hydroxyquinol 1,2-dio

49 d shown to transform 2,4,6-TCP to 6-CHQ when FADH2 was supplied by an Escherichia coli flavin reducta

50 acts as an FAD reductase to supply TcpA with FADH2, whereas the function of TcpB in 2,4,6-TCP degrada