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1 rone to the FeMo-co-deficient apo-NifDK (apo-dinitrogenase).
2 ifD1 and nifK1, which together encode the Mo dinitrogenase.
3 e the only previous example was that seen in dinitrogenase.
4 acetylene reduction ability of the resulting dinitrogenase.
5 red for its function in electron transfer to dinitrogenase.
6 r (FeMo-co) of the widely studied molybdenum-dinitrogenase.
7 omplex, forming a tight protein complex with dinitrogenase.
8 ignals of molybdenum- or vanadium-containing dinitrogenases.
9 rogenase 1 (a catalytically inactive form of dinitrogenase 1 that lacks the FeMo-co) to the FeMo-co-a
10 rogenase 2 (a catalytically inactive form of dinitrogenase 2 that lacks FeV-co) exhibit only the VNFG
11 cts of A. vinelandii strains that accumulate dinitrogenase 2, whereas extracts of strains impaired in
15 ertion mutation in vnfY has 10-fold less vnf dinitrogenase activity and exhibits a greatly diminished
16 enase reductase activity is lowered, whereas dinitrogenase activity remains essentially unaltered.
17 ected in diazotrophic growth and extractable dinitrogenase activity when cultured under conditions th
18 alancing systems, the Calvin-Benson-Bassham, dinitrogenase and dimethyl sulfoxide reductase systems,
19 vealed distinct clusters for Mo-, V-, and Fe-dinitrogenases and suggested that most methanogens also
20 ogenase when present in a 1:1 molar ratio to dinitrogenase, and 2OG fully relieved this inhibition.
21 ated between nifDK, the structural genes for dinitrogenase, and nifY, whose product is involved in ni
23 -loop of NifI(2) prevented copurification of dinitrogenase but did not affect copurification of NifI(
24 rect interaction of a NifI(1,2) complex with dinitrogenase causes inhibition, which is relieved by 2O
25 es serving as the obligate electron donor to dinitrogenase during nitrogenase turnover, dinitrogenase
27 about 23 kb from vnfDGK, which encodes the V dinitrogenase; however, like vnfDGK, vnfH was expressed
28 binding between dinitrogenase reductase and dinitrogenase; however, this change did not have a subst
31 lectron flux from dinitrogenase reductase to dinitrogenase is also surprisingly insensitive to a depl
32 synthesize FeMo-co accumulate an apo form of dinitrogenase (lacking FeMo-co), with a subunit composit
35 rving as the physiological electron donor to dinitrogenase, NifH is involved in iron-molybdenum cofac
36 o its role as the obligate electron donor to dinitrogenase, NifH is required for the iron-molybdenum
39 n paramagnetic resonance (EPR) signal of the dinitrogenase protein is not characteristic of the EPR s
43 o dinitrogenase during nitrogenase turnover, dinitrogenase reductase (NifH) is required for the biosy
45 nitrogenase reductase ADP-ribosyltransferase/dinitrogenase reductase activating glycohydrolase (DRAT/
47 of dinitrogenase reductase catalyzed by the dinitrogenase reductase ADP-ribosyl transferase (DRAT)/d
48 bolism, including GlnE, NtrB/NtrC, and DRAT (dinitrogenase reductase ADP-ribosyl transferase)-DRAG (d
49 of dinitrogenase reductase, catalyzed by the dinitrogenase reductase ADP-ribosyl transferase-dinitrog
51 cross-linking of dinitrogenase reductase and dinitrogenase reductase ADP-ribosyltransferase (DRAT) fr
52 be ADP-ribosylated or to form a complex with dinitrogenase reductase ADP-ribosyltransferase (DRAT) fr
53 ctase) activity is reversibly inactivated by dinitrogenase reductase ADP-ribosyltransferase (DraT) in
54 eductase is posttranslationally regulated by dinitrogenase reductase ADP-ribosyltransferase (DRAT) vi
55 P-ribosylation of dinitrogenase reductase by dinitrogenase reductase ADP-ribosyltransferase (DRAT).
57 ADP-ribosylation catalyzed by the DRAT-DRAG (dinitrogenase reductase ADP-ribosyltransferase-dinitroge
58 eir nitrogenase activity, independent of the dinitrogenase reductase ADP-ribosyltransferase/dinitroge
60 Lys 143 to Gln decreased the binding between dinitrogenase reductase and dinitrogenase; however, this
63 um chloride, as is the cross-linking between dinitrogenase reductase and DRAT, suggesting that ionic
68 e reduction assays, immunoblotting with anti-dinitrogenase reductase antibody, and [adenylate-(32)P]N
69 olve detectable covalent modification of the dinitrogenase reductase as in some bacteria, and the gen
70 1 is not critical for the binding of DRAT to dinitrogenase reductase but that the availability of arg
71 nslationally through the ADP-ribosylation of dinitrogenase reductase by dinitrogenase reductase ADP-r
72 pression and posttranslational regulation of dinitrogenase reductase by reversible ADP-ribosylation c
74 lation of the reversible ADP ribosylation of dinitrogenase reductase catalyzed by the dinitrogenase r
77 lation or any other covalent modification of dinitrogenase reductase during switch-off, suggesting th
78 f an arginine residue at position 101 in the dinitrogenase reductase eliminated this ADP-ribosylation
79 at both oxygen-denatured and ADP-ribosylated dinitrogenase reductase fail to form a cross-linked comp
80 -bound and adenine nucleotide-free states of dinitrogenase reductase form cross-linked complexes with
84 ither lost nitrogenase activity nor modified dinitrogenase reductase in response to darkness and NH4+
85 rogenase activity and normal modification of dinitrogenase reductase in response to NH(4)(+) and dark
90 H4+, suggesting that the ADP-ribosylation of dinitrogenase reductase is probably the only mechanism f
91 removal of the Fe(4)S(4) cluster resulted in dinitrogenase reductase not being a substrate for ADP-ri
101 ws that the ATP-dependent electron flux from dinitrogenase reductase to dinitrogenase is also surpris
102 that these changes decreased the ability of dinitrogenase reductase to form a cross-linkable complex
103 rubrum strains in which the arginine 101 of dinitrogenase reductase was replaced by tyrosine, phenyl
105 genase activity of the strain containing the dinitrogenase reductase with arginine at position 101.
107 red for FeMo-co biosynthesis (e.g. NIFNE and dinitrogenase reductase) are at the appropriate redox st
109 lum rubrum strain that lacked its endogenous dinitrogenase reductase, and they supported high nitroge
111 s-linking is specific for native, unmodified dinitrogenase reductase, in that both oxygen-denatured a
112 in nif expression or the ADP-ribosylation of dinitrogenase reductase, since a mutant expressing GS-Y3
114 G gene was used to generate altered forms of dinitrogenase reductase-activating glycohydrolase (DRAG)
115 ase reductase ADP-ribosyl transferase (DRAT)/dinitrogenase reductase-activating glycohydrolase (DRAG)
116 reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductase-activating glycohydrolase (DRAG)
118 itrogenase reductase ADP-ribosyl transferase-dinitrogenase reductase-activating glycohydrolase (DRAT-
119 nitrogenase reductase ADP-ribosyltransferase-dinitrogenase reductase-activating glycohydrolase) syste
120 ase reductase ADP-ribosyl transferase)-DRAG (dinitrogenase reductase-activating glycohydrolase).
121 ogenase reductase ADP-ribosyltransferase and dinitrogenase reductase-activating glycohydrolase, enzym
124 or NifH in the Mo nitrogenase and that these dinitrogenase reductases are not involved in determining
125 iption of the nifH1 and vnfH genes, encoding dinitrogenase reductases for the heterocyst-specific Mo-
127 e mutants and no ADP-ribosylation of altered dinitrogenase reductases occurred either in vivo or in v
128 altered nucleotide binding regions of these dinitrogenase reductases, did not significantly change t
131 esulted in copurification of NifI(1) and the dinitrogenase subunits NifD and NifK, and 2OG or a delet
132 ession of both the Calvin-Benson-Bassham and dinitrogenase systems was influenced by dimethyl sulfoxi
134 ls for extracted FeMo-co and the M center of dinitrogenase; third, site-directed mutagenesis of nafY
135 finally inserted into a pre-synthesized apo-dinitrogenase to generate mature dinitrogenase protein.
137 of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was investigated using 99Mo to follow the
139 a role in the maturation of the V-dependent dinitrogenase, with a specific role in the formation of
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