ライフサイエンスコーパス: iron-molybdenum cofactor

1 erstitial atom in the [MoFe7S9X] core of the iron-molybdenum cofactor cluster of nitrogenase.

2 We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogena

3 It has been presumed that immature iron-molybdenum cofactor-deficient nitrogenase MoFe prot

4 ermediate on the biosynthetic pathway to the iron molybdenum cofactor (FeMo-co) of nitrogenase.

5 sory factor Y) is able to bind either to the iron molybdenum cofactor (FeMo-co) or to apodinitrogenas

6 ifH) is required for the biosynthesis of the iron-molybdenum cofactor (FeMo-co) and for the maturatio

7 ent carries two complex metalloclusters, the iron-molybdenum cofactor (FeMo-co) and the [8Fe-7S] P-cl

8 n of dinitrogen to ammonium and contains the iron-molybdenum cofactor (FeMo-co) at its active site.

9 donor to dinitrogenase, NifH is involved in iron-molybdenum cofactor (FeMo-co) biosynthesis and in m

10 Iron-molybdenum cofactor (FeMo-co) biosynthesis involves

11 itrogenase maturation, having a dual role as iron-molybdenum cofactor (FeMo-co) carrier and as chaper

12 The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S,

13 uires the synthesis and the insertion of the iron-molybdenum cofactor (FeMo-co) into a presynthesized

14 The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was

15 The iron-molybdenum cofactor (FeMo-co) of nitrogenase contai

16 re some of the steps for the assembly of the iron-molybdenum cofactor (FeMo-co) of nitrogenase take p

17 The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase was in

18 o NifEN for further modification to form the iron-molybdenum cofactor (FeMo-co) of nitrogenase.

19 ted as a dinitrogen bound to the active-site iron-molybdenum cofactor (FeMo-co) of the nitrogenase Mo

20 ed are also involved in the synthesis of the iron-molybdenum cofactor (FeMo-co) of the widely studied

21 r to dinitrogenase, NifH is required for the iron-molybdenum cofactor (FeMo-co) synthesis and apodini

22 reductant is routinely added to the in vitro iron-molybdenum cofactor (FeMo-co) synthesis assay, alth

23 s an S = 1/2 EPR signal from the active-site iron-molybdenum cofactor (FeMo-co) to which are bound at

24 r, NIFH functions in the biosynthesis of the iron-molybdenum cofactor (FeMo-co), and in the processin

25 The iron-molybdenum cofactor (FeMo-co), located at the activ

26 t complex metal cofactors known to date, the iron-molybdenum cofactor (FeMo-co).

27 uces N2 at the [Fe7, Mo, S9, X, homocitrate] iron-molybdenum cofactor (FeMo-co).

28 otein contains a P cluster ([8Fe-7S]) and an iron-molybdenum cofactor (FeMoco) ([Mo-7Fe-9S-X-homocitr

29 The structures of the protein and the iron-molybdenum cofactor (FeMoco) appear to be largely u

30 However, its function in iron-molybdenum cofactor (FeMoco) biosynthesis has not b

31 y defective in its ability to participate in iron-molybdenum cofactor (FeMoco) insertion.

32 An iron-molybdenum cofactor (FeMoco) is thought to be the s

33 nterstitial carbon atom at the center of the iron-molybdenum cofactor (FeMoco) of MoFe-nitrogenase, i

34 The iron-molybdenum cofactor (FeMoco) of nitrogenase contain

35 The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the

36 e iron centers purportedly accumulate on the iron-molybdenum cofactor (FeMoco) of nitrogenase, and th

37 de-containing iron-sulfur cluster called the iron-molybdenum cofactor (FeMoco).

38 The iron-molybdenum cofactor of nitrogenase (FeMo-co) is syn

39 thermore, the identities of all atoms in the iron-molybdenum cofactor of nitrogenase have finally bee

40 onding to those reported for CO bound to the iron-molybdenum cofactor of nitrogenase were detected du

41 The properties of the Fe and Mo sites of the iron-molybdenum cofactor of nitrogenase with respect to

42 Molybdenum, as a component of the iron-molybdenum cofactor of nitrogenase, is essential fo

43 the central Fe and terminal Mo sites of the iron-molybdenum cofactor of nitrogenase.

44 transformations that may be possible at the iron-molybdenum cofactor of nitrogenases, which may have

45 The iron-molybdenum cofactor (the M-cluster) serves as the a

46 rogenase 2 is also activable in vitro by the iron-molybdenum cofactor to form a hybrid enzyme with un

47 The iron-molybdenum cofactor was unable to replace FeV-co in

48 es of the Fe and Mo sites of the nitrogenase iron-molybdenum cofactor with respect to the binding of