Spectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase

scientific article published on 01 October 1995

Spectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.270.41.24067
P698PubMed publication ID7592606

P50authorWilbur H. CampbellQ67528958
P2093author name stringN Shiraishi
R Hille
K Ratnam
P2860cites workStructural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxinQ24675963
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]Q27641437
Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domainQ27730243
Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme familyQ30195728
Nitrate reductase from squash: cDNA cloning and nitrate regulationQ33238813
Expression in Escherichia coli of Cytochrome c Reductase Activity from a Maize NADH:Nitrate Reductase Complementary DNA.Q33241939
Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductasesQ34315273
Functional domains of assimilatory nitrate reductases and nitrite reductases.Q37951284
The role of cysteine residues of spinach ferredoxin-NADP+ reductase As assessed by site-directed mutagenesis.Q38318119
Reactions of the Neurospora crassa nitrate reductase with NAD(P) analogsQ39130399
Oxidation--reduction midpoint potentials of the flavin, haem and Mo-pterin centres in spinach (Spinacia oleracea L.) nitrate reductaseQ41903098
Oxidation-reduction potentials of flavin and Mo-pterin centers in assimilatory nitrate reductase: variation with pH.Q43426626
The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductasesQ50177318
High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH:cytochrome B5 reductase.Q50880475
Measurement of the equilibrium constant of the reaction between cytochrome c and cytochrome aQ68556774
Circular dichroism and potentiometry of FAD, heme and Mo-pterin prosthetic groups of assimilatory nitrate reductaseQ69843016
One-electron oxidation-reduction properties of hepatic NADH-cytochrome b5 reductaseQ70211585
P433issue41
P407language of work or nameEnglishQ1860
P304page(s)24067-24072
P577publication date1995-10-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleSpectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase
P478volume270

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cites work (P2860)
Q46125666Analysis of wild-type and mutant plant nitrate reductase expressed in the methylotrophic yeast Pichia pastoris.
Q34812986Molybdenum enzymes in higher organisms
Q74776447Nitrate Reductase Biochemistry Comes of Age
Q43610798Pre-steady-state kinetic analysis of recombinant Arabidopsis NADH:nitrate reductase: rate-limiting processes in catalysis
Q73907271Recombinant expression of molybdenum reductase fragments of plant nitrate reductase at high levels in Pichia pastoris
Q71985148Spectroscopic and kinetic characterization of the recombinant cytochrome c reductase fragment of nitrate reductase. Identification of the rate-limiting catalytic step
Q33840734The mononuclear molybdenum enzymes