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1 fB generates an apo-MoFe protein lacking the FeMo cofactor).
2 ypes of metal centers, the P cluster and the FeMo cofactor.
3 e proximity within a specific 4Fe-4S face of FeMo cofactor.
4 n expressing this protein accumulates "free" FeMo cofactor.
5 ired for the biosynthesis of the nitrogenase FeMo cofactor.
6 species called the MoFe cluster in place of FeMo cofactor.
7 and analyze early intermediate states of the FeMo cofactor.
8 ne and allyl alcohol, bound to a nitrogenase FeMo cofactor.
9 that it contains N2 bound to the active-site FeMo cofactor.
10 tent with an N2 molecule bound end-on to the FeMo cofactor.
11 hat an N2-derived species was trapped on the FeMo cofactor.
12 from methyldiazene probably does not bind to FeMo cofactor.
13 tuted to the holo MoFe protein with isolated FeMo cofactor.
14 holo MoFe protein upon addition of isolated FeMo cofactor.
15 d that one azide binds within 200 ms to each FeMo cofactor.
16 ide and CO binding to different sites on the FeMo cofactor.
17 in the center of the catalytically essential FeMo-cofactor.
18 th a ground-state transition as observed for FeMo-cofactor.
19 se from the direct bonding of cyanide to the FeMo-cofactor.
20 ne or cyanide to a specific [4Fe-4S] face of FeMo-cofactor.
21 relaxation properties of the spin system of FeMo-cofactor.
22 -188(Cys) MoFe protein that does not contain FeMo-cofactor.
23 r, respectively designated the P-cluster and FeMo-cofactor.
24 es within the polypeptide environment of the FeMo-cofactor.
25 w that the apo-MoFe protein does not contain FeMo-cofactor.
26 Fe protein value by the addition of isolated FeMo-cofactor.
27 studied the binding of CO to the active-site FeMo-cofactor.
28 that mimics the mechanism of the nitrogenase FeMo-cofactor.
29 ains; and the asymmetric displacement of the FeMo-cofactor.
30 hi-CO state, with two CO molecules bound to FeMo-cofactor.
31 ls a CO molecule bridging Fe2 and Fe6 of the FeMo-cofactor.
32 mmetric breathing of the central cage of the FeMo-cofactor.
33 molybdenum as the site of N2 binding in the FeMo-cofactor.
34 eathing" modes similar to those seen for the FeMo-cofactor.
35 of a diazene-derived [-NHx] moiety bound to FeMo-cofactor.
36 ediating intercomponent electron transfer to FeMo-cofactor.
37 ing to an eta(2) coordination at Fe-6 of the FeMo-cofactor.
38 bound substrate-derived intermediate on the FeMo-cofactor.
39 (2)) interact with the same Fe-S face of the FeMo-cofactor.
40 cluster in the nitrogenase MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-homocitrate-X]; FeMo-co) only
41 bind and react at Fe ions of the active-site FeMo-cofactor [7Fe-9S-C-Mo-homocitrate] contained within
42 ntains the active site metallocluster called FeMo-cofactor [7Fe-9S-Mo-homocitrate] that exhibits an S
43 of the MoFe protein contains the polynuclear FeMo cofactor, a species composed of seven iron atoms, o
44 on nitrogenases reduce atmospheric N2 at the FeMo cofactor, a sulfur-rich iron-molybdenum cluster (Fe
46 ridging CO ligand between Fe2 and Fe6 of the FeMo-cofactor, a new ligand binding mode is revealed thr
47 tantial and reversible reorganization of the FeMo-cofactor accompanying CO binding was unanticipated
48 of steel", stabilizing the structure of the FeMo-cofactor-active site during nitrogenase catalysis.
50 The nature of the intermediates bound to FeMo-cofactor along this reduction pathway remains unkno
51 ble of supporting substrate reduction at the FeMo cofactor and provide important insights into the ge
55 of propargyl alcohol to one [4Fe-4S] face of FeMo-cofactor and indicate roles for the alpha-70(Val) r
56 oFe protein having one alphabeta-unit with a FeMo-cofactor and mature P-cluster and the other alphabe
57 luded fully active MoFe protein replete with FeMo-cofactor and mature P-cluster, inactive MoFe protei
58 e P-cluster, inactive MoFe protein having no FeMo-cofactor and only immature P-cluster, and partially
60 of the hydrogen-bonding interactions between FeMo-cofactor and polypeptide environment has not yet be
61 f an NuH-S hydrogen bond interaction between FeMo-cofactor and the imidazole side chain of alpha-His(
62 tion environment that mimics the nitrogenase FeMo-cofactor and was recently shown to provide state-of
63 inhibitors at the active-site metal cluster FeMo cofactor, and finally, considerations of the mechan
64 ncorporation of sulfur and selenium into the FeMo cofactor, and to assign hyperfine couplings of (33)
65 tioning of side chains along one side of the FeMo-cofactor, and the corresponding EPR data shows a ne
66 ve site; alpha-70 approaches one face of the FeMo-cofactor, and when valine is substituted by alanine
67 idues, can eliminate the N1 interaction with FeMo-cofactor; and (iv) ESEEM can be used to detect slig
68 was localized to a specific Fe-S face of the FeMo-cofactor approached by the MoFe protein amino acid
69 good diazotrophic growth and also contained FeMo cofactor as indicated by its biologically unique S
70 es are likely to be remote from the proposed FeMo cofactor assembly site and are unlikely to become i
71 [FeFe]-hydrogenase H cluster and nitrogenase FeMo-cofactor assembly in the context of these emerging
74 e displacement of S2B and distortions of the FeMo-cofactor at the E(0)-E(3) intermediates of the subs
77 educe that the Fe protein interacts with the FeMo cofactor-binding alpha-subunit of the MoFe protein.
79 e protein is fully functional in an in vitro FeMo cofactor biosynthesis assay, and the strain express
80 that are critical to its functions in either FeMo cofactor biosynthesis or FeMo cofactor insertion.
82 roduced and purified in this way exhibits an FeMo cofactor biosynthetic activity similar to that prev
83 95-histidine provides a hydrogen bond to the FeMo-cofactor but is not the source of the 14N1 modulati
84 enase requires a reductive activation of the FeMo-cofactor, but the precise structure and atomic comp
86 red for acceptance of the negatively charged FeMo cofactor by the separately synthesized, cofactor-de
87 turned over with hydrazine as substrate, the FeMo-cofactor can be freeze-trapped in a S = (1)/(2) sta
88 eted to indicate that the 4Fe-4S face of the FeMo cofactor capped by the alpha-subunit Val(70) residu
89 CO-inhibited hi-CO the dominant role of the FeMo-cofactor carbide is to maintain the core structure,
90 may be an important proton conductor to the FeMo cofactor center and specifically required for reduc
93 e the N coordination of the iron-molybdenum (FeMo) cofactor contained within the nitrogenase MoFe pro
94 tylene and cyanide are able to interact with FeMo-cofactor contained within the alpha-96-substituted
98 turbations to the inorganic framework of the FeMo-cofactor; depletion of the homocitrate moiety; dimi
99 specificities, reinforced by changes in the FeMo-cofactor-derived S = 3/2 EPR spectrum, clearly indi
100 t influences the electronic structure of the FeMo cofactor, dictating preferred orientations of possi
101 f HCA is coupled to alpha-subunit domain and FeMo-cofactor disordering, and formation of a histidine
106 no acid substitutions within the active site FeMo-cofactor environment was examined by Fourier transf
107 genase, with amino acid substitutions in the FeMo-cofactor environment, were used to probe interactio
108 lting in the conversion of the resting-state FeMo-cofactor EPR signal (S = 3/2 and g = [4.41, 3.60, 2
109 lpha-96(Leu) MoFe protein also decreased the FeMo-cofactor EPR signal with concomitant appearance of
110 markedly different from those of the classic FeMo-cofactor EPR signal, consistent with the difference
112 modulation of a belt Fe-C interaction in the FeMo-cofactor facilitates substrate binding and reductio
115 four reducing equivalents at the active-site FeMo-cofactor (FeMo-co), generating a state (denoted E(4
117 a, have made a detailed understanding of the FeMo cofactor (FeMoco) active site electronic structure
121 cluster that models a cubane portion of the FeMo cofactor (FeMoco), including a bridging carbyne lig
123 rtner, Fe protein, is also required for both FeMo-cofactor formation and the conversion of an immatur
125 catalysis by facilitating activation of the FeMo-cofactor from a relatively stable form to a state c
126 selective incorporation of selenium into the FeMo-cofactor from selenocyanate as a newly identified s
127 of activating apo-dinitrogenase (lacking the FeMo cofactor) from Azotobacter vinelandii was extracted
128 clusters with the MoFe(3)S(3) subunit of the FeMo-cofactor has led to the suggestion that the storage
129 bits a signal (S(EPR1)) originating from the FeMo-cofactor having two or more bound C(2)H(2) adducts
130 -derived species is bound to the active-site FeMo cofactor; (ii) this species binds through an [-NHx]
131 ter in the iron (Fe) protein component to an FeMo cofactor in the molybdenum-iron (MoFe) protein comp
132 el for the structure of the iron-molybdenum (FeMo)-cofactor in the S = (1)/(2) state trapped during t
136 e reveals selenium occupying the S2B site of FeMo-cofactor in the Azotobacter vinelandii MoFe-protein
137 pha-96(Arg)) located next to the active site FeMo-cofactor in the MoFe protein by leucine, glutamine,
138 chemical environment around the active site FeMo-cofactor in the MoFe protein, either by substitutin
141 tes a hydrazine-derived species bound to the FeMo-cofactor; in spectra taken at g(1) this species giv
142 type and E146D Fe proteins to participate in FeMo cofactor insertion demonstrate, however, that the m
145 rby amino acids or transferring the isolated FeMo-cofactor into a different peptide matrix, changes t
146 f the inert resting state of the active site FeMo-cofactor into an activated state capable of reducin
148 r the alpha beta subunit pair that lacks the FeMo cofactor is altered and that the change is recogniz
151 f nitrogenase, the [Mo:7Fe:9S:C]:homocitrate FeMo cofactor, is a S=3/2 system with a rhombic magnetic
152 EN complex, the site for biosynthesis of the FeMo cofactor, is an alpha2beta2 tetramer that is struct
156 interaction of substrates or inhibitors with FeMo-cofactor occurs as a consequence of both increased
157 the discovery of interstitial carbide in the FeMo cofactor of Mo-dependent nitrogenase, but has prove
158 The H cluster of [FeFe]-hydrogenases and the FeMo cofactor of Mo-nitrogenase require specific maturat
159 Y is shown here to be capable of binding the FeMo cofactor of nitrogenase but unable to bind to apodi
161 The M(N) S = (3)/(2) resting state of the FeMo cofactor of nitrogenase has been proposed to have m
162 h the monoprotonated dinitrogen bound to the FeMo cofactor of nitrogenase up to the formation of the
163 scent of the proposed N2 binding step at the FeMo cofactor of nitrogenase, suggesting the use of the
164 of acetylene with its binding site(s) on the FeMo cofactor of the MoFe protein of Azotobacter vinelan
165 his study, selenium- and sulfur-incorporated FeMo cofactors of the catalytic MoFe protein component f
169 cture with two CO ligands coordinated to the FeMo-cofactor of the molybdenum nitrogenase at 1.33 A re
170 d by blocking the misincorporation of either FeMo-cofactor or FeV-cofactor during its maturation.
171 otein, and the [8Fe-7S] (or P-) clusters and FeMo cofactors (or M-centers) of the MoFe protein, were
173 tution of other amino acids located near the FeMo-cofactor, or by changing the partial pressure of CO
174 iously characterized counterparts around the FeMo-cofactor, oxidized Gd-MoFeP features an unusual Tyr
175 n established that the N coordination of the FeMo cofactor provided by the MoFe-protein polypeptide m
177 ed density around the S2B belt sulfur of the FeMo-cofactor; rearrangements of cluster-adjacent side c
179 inelandii, showed that the N coordination to FeMo cofactor requires His-195 of the MoFe protein alpha
180 e-derived intermediate can be trapped on the FeMo-cofactor resulting in an S = 1/2 spin system with a
183 rotein decreased the intensity of the normal FeMo-cofactor signal with the appearance of a new EPR si
185 MoFe protein molecules that contain only one FeMo cofactor site occupied and provides a rationale for
186 is process releases H2, yielding N2 bound to FeMo-cofactor that is doubly reduced relative to the res
187 o crudely model a single-belt Fe site of the FeMo-cofactor that might bind N2 at a position trans to
188 (N2) to two ammonia (NH3) at its active site FeMo-cofactor through a mechanism involving reductive el
189 ch is one of only two residues anchoring the FeMo cofactor to the polypeptide, and (ii) a component o
190 70) residue is the most likely region within FeMo cofactor to which acetylene binds with high affinit
191 d in conversion of the S = 3/2 resting state FeMo-cofactor to a novel S = 1/2 state with g1 = 2.09, g
194 uished by a heterometal site occupied by Mo (FeMo-cofactor), V (FeV-cofactor), or Fe (FeFe-cofactor).
195 64, 2.00]) arising from the resting state of FeMo cofactor was observed to convert to a rhombic, S =
196 mino acid substitutions near the site of its FeMo cofactor was recently described as having the capac
198 the hydrazine-derived [-NHx] moiety bound to FeMo-cofactor when the same MoFe protein is trapped duri
199 reduction of substrates, may occur with the FeMo-cofactor, which also appears to have M-M bonding.
200 a 7Fe-9S-Mo-C-homocitrate species designated FeMo-cofactor, which provides the N(2)-binding catalytic
201 (7)S(9)C-(R)-homocitrate] species designated FeMo-cofactor, whose biosynthesis and insertion requires
202 2 revealed a 15N nuclear spin coupled to the FeMo cofactor with a hyperfine tensor A = [0.9, 1.4, 0.4
204 n be used to detect slight reorientations of FeMo-cofactor within its polypeptide pocket, although th
205 E(4)(2H)* state containing a doubly reduced FeMo-cofactor without Fe-bound substrates; and (vii) pro
206 of four electrons/protons on its active site FeMo-cofactor, yielding a state, designated as E4, which