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1    Conformational changes near the catalytic iron-molybdenum cofactor are correlated with the nucleot
2 erstitial atom in the [MoFe7S9X] core of the iron-molybdenum cofactor cluster of nitrogenase.
3 We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogena
4           It has been presumed that immature iron-molybdenum cofactor-deficient nitrogenase MoFe prot
5 ermediate on the biosynthetic pathway to the iron molybdenum cofactor (FeMo-co) of nitrogenase.
6 sory factor Y) is able to bind either to the iron molybdenum cofactor (FeMo-co) or to apodinitrogenas
7 ifH) is required for the biosynthesis of the iron-molybdenum cofactor (FeMo-co) and for the maturatio
8 ent carries two complex metalloclusters, the iron-molybdenum cofactor (FeMo-co) and the [8Fe-7S] P-cl
9 n of dinitrogen to ammonium and contains the iron-molybdenum cofactor (FeMo-co) at its active site.
10  donor to dinitrogenase, NifH is involved in iron-molybdenum cofactor (FeMo-co) biosynthesis and in m
11                                              Iron-molybdenum cofactor (FeMo-co) biosynthesis involves
12 itrogenase maturation, having a dual role as iron-molybdenum cofactor (FeMo-co) carrier and as chaper
13      The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S,
14 uires the synthesis and the insertion of the iron-molybdenum cofactor (FeMo-co) into a presynthesized
15                      The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was
16                                          The iron-molybdenum cofactor (FeMo-co) of nitrogenase contai
17 re some of the steps for the assembly of the iron-molybdenum cofactor (FeMo-co) of nitrogenase take p
18                      The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase was in
19 o NifEN for further modification to form the iron-molybdenum cofactor (FeMo-co) of nitrogenase.
20 ted as a dinitrogen bound to the active-site iron-molybdenum cofactor (FeMo-co) of the nitrogenase Mo
21 ed are also involved in the synthesis of the iron-molybdenum cofactor (FeMo-co) of the widely studied
22 r to dinitrogenase, NifH is required for the iron-molybdenum cofactor (FeMo-co) synthesis and apodini
23 reductant is routinely added to the in vitro iron-molybdenum cofactor (FeMo-co) synthesis assay, alth
24 s an S = 1/2 EPR signal from the active-site iron-molybdenum cofactor (FeMo-co) to which are bound at
25 r, NIFH functions in the biosynthesis of the iron-molybdenum cofactor (FeMo-co), and in the processin
26                                          The iron-molybdenum cofactor (FeMo-co), located at the activ
27 t complex metal cofactors known to date, the iron-molybdenum cofactor (FeMo-co).
28 uces N2 at the [Fe7, Mo, S9, X, homocitrate] iron-molybdenum cofactor (FeMo-co).
29 otein contains a P cluster ([8Fe-7S]) and an iron-molybdenum cofactor (FeMoco) ([Mo-7Fe-9S-X-homocitr
30        The structures of the protein and the iron-molybdenum cofactor (FeMoco) appear to be largely u
31                     However, its function in iron-molybdenum cofactor (FeMoco) biosynthesis has not b
32 y defective in its ability to participate in iron-molybdenum cofactor (FeMoco) insertion.
33                                           An iron-molybdenum cofactor (FeMoco) is thought to be the s
34 nterstitial carbon atom at the center of the iron-molybdenum cofactor (FeMoco) of MoFe-nitrogenase, i
35                                          The iron-molybdenum cofactor (FeMoco) of nitrogenase contain
36                            The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the
37 e iron centers purportedly accumulate on the iron-molybdenum cofactor (FeMoco) of nitrogenase, and th
38 de-containing iron-sulfur cluster called the iron-molybdenum cofactor (FeMoco).
39                                          The iron-molybdenum cofactor of nitrogenase (FeMo-co) is syn
40                                          The iron-molybdenum cofactor of nitrogenase (FeMoco) catalyz
41 thermore, the identities of all atoms in the iron-molybdenum cofactor of nitrogenase have finally bee
42 onding to those reported for CO bound to the iron-molybdenum cofactor of nitrogenase were detected du
43 The properties of the Fe and Mo sites of the iron-molybdenum cofactor of nitrogenase with respect to
44            Molybdenum, as a component of the iron-molybdenum cofactor of nitrogenase, is essential fo
45  the central Fe and terminal Mo sites of the iron-molybdenum cofactor of nitrogenase.
46  transformations that may be possible at the iron-molybdenum cofactor of nitrogenases, which may have
47                                          The iron-molybdenum cofactor (the M-cluster) serves as the a
48 rogenase 2 is also activable in vitro by the iron-molybdenum cofactor to form a hybrid enzyme with un
49                                          The iron-molybdenum cofactor was unable to replace FeV-co in
50 es of the Fe and Mo sites of the nitrogenase iron-molybdenum cofactor with respect to the binding of