ライフサイエンスコーパス: dinitrogenase reductase

1 regulated by reversible ADP-ribosylation of dinitrogenase reductase.

2 exhibited an EPR spectrum characteristic of dinitrogenase reductases.

3 nitrogenase reductase ADP-ribosyltransferase/dinitrogenase reductase activating glycohydrolase (DRAT/

4 The ADP-ribosyl is removed by the dinitrogenase reductase-activating glycohydrolase (DraG)

5 G gene was used to generate altered forms of dinitrogenase reductase-activating glycohydrolase (DRAG)

6 ase reductase ADP-ribosyl transferase (DRAT)/dinitrogenase reductase-activating glycohydrolase (DRAG)

7 reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductase-activating glycohydrolase (DRAG)

8 Association of dinitrogenase reductase-activating glycohydrolase (DRAG)

9 itrogenase reductase ADP-ribosyl transferase-dinitrogenase reductase-activating glycohydrolase (DRAT-

10 nitrogenase reductase ADP-ribosyltransferase-dinitrogenase reductase-activating glycohydrolase) syste

11 ase reductase ADP-ribosyl transferase)-DRAG (dinitrogenase reductase-activating glycohydrolase).

12 ogenase reductase ADP-ribosyltransferase and dinitrogenase reductase-activating glycohydrolase, enzym

13 In these mutants, dinitrogenase reductase activity is lowered, whereas din

14 Fe protein (dinitrogenase reductase) activity is reversibly inactiva

15 of dinitrogenase reductase catalyzed by the dinitrogenase reductase ADP-ribosyl transferase (DRAT)/d

16 bolism, including GlnE, NtrB/NtrC, and DRAT (dinitrogenase reductase ADP-ribosyl transferase)-DRAG (d

17 of dinitrogenase reductase, catalyzed by the dinitrogenase reductase ADP-ribosyl transferase-dinitrog

18 The nitrogenase-regulating enzymes dinitrogenase reductase ADP-ribosyltransferase (DRAT) an

19 be ADP-ribosylated or to form a complex with dinitrogenase reductase ADP-ribosyltransferase (DRAT) fr

20 cross-linking of dinitrogenase reductase and dinitrogenase reductase ADP-ribosyltransferase (DRAT) fr

21 ctase) activity is reversibly inactivated by dinitrogenase reductase ADP-ribosyltransferase (DraT) in

22 eductase is posttranslationally regulated by dinitrogenase reductase ADP-ribosyltransferase (DRAT) vi

23 P-ribosylation of dinitrogenase reductase by dinitrogenase reductase ADP-ribosyltransferase (DRAT).

24 The dra operon encodes dinitrogenase reductase ADP-ribosyltransferase and dinit

25 ADP-ribosylation catalyzed by the DRAT-DRAG (dinitrogenase reductase ADP-ribosyltransferase-dinitroge

26 eir nitrogenase activity, independent of the dinitrogenase reductase ADP-ribosyltransferase/dinitroge

27 These mutated dinitrogenase reductases also were expressed in a Rhodos

28 Chemical cross-linking of dinitrogenase reductase and dinitrogenase reductase ADP-

29 Lys 143 to Gln decreased the binding between dinitrogenase reductase and dinitrogenase; however, this

30 Cross-linking between dinitrogenase reductase and DRAT requires the presence o

31 The R101F form of dinitrogenase reductase and DRAT together were not able

32 um chloride, as is the cross-linking between dinitrogenase reductase and DRAT, suggesting that ionic

33 ubstantial effect on the interaction between dinitrogenase reductase and DRAT.

34 significantly change the interaction between dinitrogenase reductase and DRAT.

35 reaction, does support cross-linking between dinitrogenase reductase and DRAT.

36 It is also possible that dinitrogenase reductase and/or NIFNE (both Fe-S proteins

37 lum rubrum strain that lacked its endogenous dinitrogenase reductase, and they supported high nitroge

38 The alternative dinitrogenase reductase (ANF2) was purified as an alpha2

39 e reduction assays, immunoblotting with anti-dinitrogenase reductase antibody, and [adenylate-(32)P]N

40 or NifH in the Mo nitrogenase and that these dinitrogenase reductases are not involved in determining

41 red for FeMo-co biosynthesis (e.g. NIFNE and dinitrogenase reductase) are at the appropriate redox st

42 olve detectable covalent modification of the dinitrogenase reductase as in some bacteria, and the gen

43 1 is not critical for the binding of DRAT to dinitrogenase reductase but that the availability of arg

44 nslationally through the ADP-ribosylation of dinitrogenase reductase by dinitrogenase reductase ADP-r

45 pression and posttranslational regulation of dinitrogenase reductase by reversible ADP-ribosylation c

46 Both DRAT and dinitrogenase reductase can be labeled by [carbonyl-(14)

47 lation of the reversible ADP ribosylation of dinitrogenase reductase catalyzed by the dinitrogenase r

48 Reversible ADP-ribosylation of dinitrogenase reductase, catalyzed by the dinitrogenase

49 as the transcriptional regulator SoxR or the dinitrogenase reductase component of nitrogenase.

50 R140Q dinitrogenase reductase could not be ADP-ribosylated by

51 altered nucleotide binding regions of these dinitrogenase reductases, did not significantly change t

52 lation or any other covalent modification of dinitrogenase reductase during switch-off, suggesting th

53 f an arginine residue at position 101 in the dinitrogenase reductase eliminated this ADP-ribosylation

54 at both oxygen-denatured and ADP-ribosylated dinitrogenase reductase fail to form a cross-linked comp

55 iption of the nifH1 and vnfH genes, encoding dinitrogenase reductases for the heterocyst-specific Mo-

56 -bound and adenine nucleotide-free states of dinitrogenase reductase form cross-linked complexes with

57 In this study, mutant forms of dinitrogenase reductase from A. vinelandii that are affe

58 The structure of the dinitrogenase reductase from Azotobacter vinelandii is k

59 Altered dinitrogenase reductases from strains UR629 (R101Y) and

60 NifH (dinitrogenase reductase) has three important roles in th

61 and in the ability to recognize variants of dinitrogenase reductase have been found.

62 ither lost nitrogenase activity nor modified dinitrogenase reductase in response to darkness and NH4+

63 rogenase activity and normal modification of dinitrogenase reductase in response to NH(4)(+) and dark

64 s-linking is specific for native, unmodified dinitrogenase reductase, in that both oxygen-denatured a

65 Conformational changes in dinitrogenase reductase induced by an F135Y substitution

66 AT; however, cross-linking is inhibited when dinitrogenase reductase is in its ATP-bound state.

67 The DRAT-catalyzed ADP-ribosylation of dinitrogenase reductase is inhibited by sodium chloride,

68 Dinitrogenase reductase is posttranslationally regulated

69 H4+, suggesting that the ADP-ribosylation of dinitrogenase reductase is probably the only mechanism f

70 o dinitrogenase during nitrogenase turnover, dinitrogenase reductase (NifH) is required for the biosy

71 (the metabolic product of NifB), NifNE, and dinitrogenase reductase (NifH).

72 removal of the Fe(4)S(4) cluster resulted in dinitrogenase reductase not being a substrate for ADP-ri

73 e mutants and no ADP-ribosylation of altered dinitrogenase reductases occurred either in vivo or in v

74 The nifH1 gene, which encodes the dinitrogenase reductase of the Mo nitrogenase that is ex

75 The vnfH gene, which encodes the dinitrogenase reductase of the V nitrogenase, was locate

76 Thus, the Arg 140 residue of dinitrogenase reductase plays a critical role in the ADP

77 Although ADP-ribosylation of dinitrogenase reductase plays a significant role in the

78 reversible covalent ADP-ribosylation of the dinitrogenase reductase protein, NifH.

79 t nitrogenase 2 (vnf-encoded) has a distinct dinitrogenase reductase protein, VNFH.

80 These results suggest that the dinitrogenase reductase proteins do not specify the hete

81 The strain containing the R101F form of dinitrogenase reductase retains 91%, the strain containi

82 in nif expression or the ADP-ribosylation of dinitrogenase reductase, since a mutant expressing GS-Y3

83 The ability of R101F dinitrogenase reductase to be labeled by [carbonyl-(14)C

84 ws that the ATP-dependent electron flux from dinitrogenase reductase to dinitrogenase is also surpris

85 that these changes decreased the ability of dinitrogenase reductase to form a cross-linkable complex

86 rubrum strains in which the arginine 101 of dinitrogenase reductase was replaced by tyrosine, phenyl

87 The R101F and R101Y forms of dinitrogenase reductase were able to form a complex with

88 genase activity of the strain containing the dinitrogenase reductase with arginine at position 101.