The effect of lysine- and arginine-modifying reagents on spinach ferredoxin: nitrite oxidoreductase

Hirasawa, Masakazu; Best, Jappe H. de; Knaff, David B.

doi:10.1016/0005-2728(93)90070-v

Cited by 29 publications

(11 citation statements)

References 33 publications

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“…The CD spectrum was first measured for the wild-type recombinant enzyme in the region from 300 nm to 650 nm, where the asymmetric environments of the prosthetic groups give rise to CD features. This spectrum (not shown) is similar to that previously measured for the enzyme isolated from spinach leaf (Hirasawa et al 1993), except that the magnitude of the broad feature centered at 580 nm is larger for the recombinant enzyme than for the leaf enzyme. Thus, there may be some small differences in the environments of the prosthetic groups in the leaf and recombinant enzymes.…”

Section: Resultssupporting

confidence: 74%

“…The alpha-helix and beta-sheet contents of wild-type and mutated recombinant enzyme were calculated from CD spectra as described by Sreerama and Woody (2004). Assays of nitrite reductase activity with either reduced ferredoxin or with reduced methyl viologen serving as the electron donor were carried out as described previously (Hirasawa et al 1993). Chemical modification of nitrite reductase tryptophan residues by treatment with N-bromosuccinimide (NBS) was carried out as described previously (Hirasawa et al 1994b).…”

Section: Methodsmentioning

confidence: 99%

“…Nitrite reductase was isolated from spinach leaves and purified to homogeneity as described previously (Hirasawa et al 1993). Absorbance spectra were obtained using a Shimadzu UV-2401 PC spectrophotometer at 1.0 nm spectral resolution.…”

Section: Methodsmentioning

confidence: 99%

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The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

et al. 2007

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A system has been developed for expressing a His-tagged form of the ferredoxin-dependent nitrite reductase of spinach in Escherichia coli. The catalytic and spectral properties of the His-tagged, recombinant enzyme are similar, but not identical, to those previously observed for nitrite reductase isolated directly from spinach leaf. A detailed comparison of the spectral, catalytic and fluorescence properties of nitrite reductase variants, in which each of the enzyme's eight tryptophan residues has been replaced using site-directed mutagenesis by either aromatic or non-aromatic amino acids, has been used to examine possible roles for tryptophan residues in the reduction of nitrite to ammonia catalyzed by the enzyme.

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Section: Resultssupporting

confidence: 74%

Section: Methodsmentioning

confidence: 99%

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The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

et al. 2007

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“…Bean sprout ferredoxin (A421 nm/A277nm ~-0.45), spinach leaf ferredoxin (A422 nm/A277 nm ----0.45) and spinach leaf nitrite reductase were prepared as described previously [5,8,9] and stored at liquid nitrogen temperature. Acetyl CoA, succinyl CoA, fl-mercaptoethanol, 2,4-dinitrophenylhydrazine, phenylmethylsulfonyl fluoride (PMSF), t-amylalcohol, sodium pyruvate, bovine serum albumin, Sigmacell Type 100 cellulose polyester thin layer chromatography sheets, and [14C]sodium bicarbonate were purchased from Sigma Chemical Co.…”

Section: Methodsmentioning

confidence: 99%

Ferrodoxin‐dependent CO₂ fixation in bean sprouts

et al. 1995

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Extracts of bean sprouts are capable of reducing ferredoxin and of catalyzing the incorporation of bicarbonate and acetyl coenzyme A into an organic compound that is likely to be pyruvate, in a reaction that requires reduced ferredoxin. The rate of the reaction, the first known for which ferredoxin appears to serve as the direct reductant for CO 2 fixation in a higher plant, depends on the concentrations of both ferredoxin and bicarbonate, with half-maximal rates being observed at ferredoxin and bicarbonate concentrations of 0.8 ttM and 200/~M, respectively.

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“…Reduced ferredoxin is the physiological electron donor and is believed to bind to a conserved region in the N-terminal part of the protein. Treatment of spinach ferredoxin-dependent NiR with lysine-or arginine-modifying reagents has been shown to inhibit ferredoxin binding, implicating the involvement of such residues in ferredoxin binding [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

Structure and expression of a nitrite reductase gene from bean (Phaseolus vulgaris) and promoter analysis in transgenic tobacco

Sander¹,

Jensen²,

Back³

et al. 1995

Plant Mol Biol

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A structural gene encoding nitrite reductase (NiR) in bean (Phaseolus vulgaris) has been cloned and sequenced. The NiR gene is present as a single copy encoding a protein of 582 amino acids. The bean NiR protein is synthesized as a precursor with an amino-terminal transit peptide (TP) consisting of 18 amino acid residues. The bean NiR transit peptide shows similarity to the TPs of other known plant NiRs. The NiR gene is expressed in trifoliate leaves and in roots of 20-day old bean plants where transcript accumulation is nitrate-inducible. Gene expression occurs in a circadian rhythm and induced by light in leaves of dark-adapted plants. A particular 100 bp sequence is present in the promoter and in the first intron of the NiR gene. Several copies of this 100 bp sequence are present in the bean genome. Comparisons between the promoter of the bean NiR gene and of two bean nitrate reductase genes (NR1 and NR2) show a limited number of conserved motifs, although the genes are presumed to be co-regulated. Comparisons are also made between the bean NiR promoter and the spinach NiR promoter. Transformation of tobacco plants with the bean NiR promoter fused to the GUS reporter gene (beta-glucuronidase) shows that the bean NiR promoter is nitrate-regulated and that the presence of the 100 bp sequence influences the level of GUS activity. NiR-coding sequences are not required for nitrate regulation but have a quantitative effect on the measured GUS activity.

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The effect of lysine- and arginine-modifying reagents on spinach ferredoxin: nitrite oxidoreductase

Cited by 29 publications

References 33 publications

The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

Ferrodoxin‐dependent CO₂ fixation in bean sprouts

Structure and expression of a nitrite reductase gene from bean (Phaseolus vulgaris) and promoter analysis in transgenic tobacco

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The effect of lysine- and arginine-modifying reagents on spinach ferredoxin: nitrite oxidoreductase

Cited by 29 publications

References 33 publications

The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

Ferrodoxin‐dependent CO2 fixation in bean sprouts

Structure and expression of a nitrite reductase gene from bean (Phaseolus vulgaris) and promoter analysis in transgenic tobacco

Contact Info

Product

Resources

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Ferrodoxin‐dependent CO₂ fixation in bean sprouts