PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10683447-2 2000 Electrochemical and fluorometric measurements both showed that NO is produced by corn NR in the presence of nitrite and NADH at pH 7. NAD 120-124 nitrate reductase [NADH] 1 Zea mays 86-88 12228428-4 1995 Asparagine (1 mM) or glutamine (1 mM), potential products of that hydrolysis, inhibited the induction of NADH-dependent root NR in the dry system by about 70%. NAD 105-109 nitrate reductase [NADH] 1 Zea mays 125-127 16667591-3 1990 Two forms of NR were identified, an NADH monospecific NR found mainly in the 1cm root tip and an NAD(P)H bispecific NR found predominantly in mature regions of the root. NAD 36-40 nitrate reductase [NADH] 1 Zea mays 13-15 7812715-5 1994 This catalytically competent fragment of nitrate reductase consists of two domains, the amino-terminal lobe, which binds FAD, and the carboxy-terminal lobe, which presumably binds NADH, connected by a linker region. NAD 180-184 nitrate reductase [NADH] 1 Zea mays 41-58 16668941-6 1992 The purified cytochrome c reductase, which had a major size of 43 kilodaltons, was inhibited by polyclonal antibodies for maize leaf NADH:nitrate reductase and bound these antibodies when blotted to nitrocellulose. NAD 133-137 nitrate reductase [NADH] 1 Zea mays 138-155 16668941-7 1992 Ultraviolet and visible spectra of oxidized and NADH-reduced recombinant cytochrome c reductase were nearly identical with those of maize leaf NADH:nitrate reductase. NAD 48-52 nitrate reductase [NADH] 1 Zea mays 148-165 16668941-0 1992 Expression in Escherichia coli of Cytochrome c Reductase Activity from a Maize NADH:Nitrate Reductase Complementary DNA. NAD 79-83 nitrate reductase [NADH] 1 Zea mays 84-101 16668941-2 1992 Zmnr1S was shown to be an NADH:nitrate reductase clone by nucleotide sequencing and comparison of its deduced amino acid sequence to Zmnr1. NAD 26-30 nitrate reductase [NADH] 1 Zea mays 31-48 16668941-4 1992 The cell lysate contained NADH:cytochrome c reductase activity, which is a characteristic partial activity of NADH:nitrate reductase dependent on the cytochrome b and flavin adenine dinucleotide domains. NAD 26-30 nitrate reductase [NADH] 1 Zea mays 115-132 16668941-4 1992 The cell lysate contained NADH:cytochrome c reductase activity, which is a characteristic partial activity of NADH:nitrate reductase dependent on the cytochrome b and flavin adenine dinucleotide domains. NAD 110-114 nitrate reductase [NADH] 1 Zea mays 115-132 16664639-1 1986 NADH:nitrate reductase was extracted from corn leaves (Zea mays L. W64A x W182E) and purified on blue Sepharose. NAD 0-4 nitrate reductase [NADH] 1 Zea mays 5-22 16665101-1 1986 Bromphenol blue, which was reduced with dithionite, was found to support nitrate reduction catalyzed by squash NADH:nitrate reductase at a rate about 5 times greater than NADH with freshly prepared enzyme and 10 times or more with enzyme having been frozen and thawed. NAD 111-115 nitrate reductase [NADH] 1 Zea mays 116-133 16665101-1 1986 Bromphenol blue, which was reduced with dithionite, was found to support nitrate reduction catalyzed by squash NADH:nitrate reductase at a rate about 5 times greater than NADH with freshly prepared enzyme and 10 times or more with enzyme having been frozen and thawed. NAD 171-175 nitrate reductase [NADH] 1 Zea mays 116-133 16665101-5 1986 When squash NADH:nitrate reductase activity was inactivated with p-hydroxymercuribenzoate or denatured by heating at 40 degrees C, the bromphenol blue nitrate reductase activity was not lost. NAD 12-16 nitrate reductase [NADH] 1 Zea mays 17-34 16665101-5 1986 When squash NADH:nitrate reductase activity was inactivated with p-hydroxymercuribenzoate or denatured by heating at 40 degrees C, the bromphenol blue nitrate reductase activity was not lost. NAD 12-16 nitrate reductase [NADH] 1 Zea mays 151-168 16665054-3 1986 We demonstrate in this work that scutella of very young maize seedlings contain NADH NR almost exclusively and that this activity is gradually replaced, as the seedling ages, with NAD(P)H NR. NAD 80-84 nitrate reductase [NADH] 1 Zea mays 85-87 16665054-4 1986 Leaves in the seedlings contain exclusively the NADH NR activity. NAD 48-52 nitrate reductase [NADH] 1 Zea mays 53-55 16665054-9 1986 The same pattern of NADH NR and NAD(P)H NR activities was found in unorganized as well as in organized callus, in recognizable root-like and even in green shoot-like material, both activities being present in all these tissues. NAD 20-24 nitrate reductase [NADH] 1 Zea mays 25-27 16665054-10 1986 An examination of the NR complement in different organs of a number of siblings originating from a cross involving transposon Mu-containing parents and having different levels of leaf NADH NR activity shows that the leaf NADH NR activity content and the scutellum NAD(P)H NR activity content are relatively independent of each other, indicating that the genetic programs specifying the NR content of these organs are not tightly coupled, if at all. NAD 184-188 nitrate reductase [NADH] 1 Zea mays 189-191 16665054-10 1986 An examination of the NR complement in different organs of a number of siblings originating from a cross involving transposon Mu-containing parents and having different levels of leaf NADH NR activity shows that the leaf NADH NR activity content and the scutellum NAD(P)H NR activity content are relatively independent of each other, indicating that the genetic programs specifying the NR content of these organs are not tightly coupled, if at all. NAD 184-188 nitrate reductase [NADH] 1 Zea mays 189-191 16665054-10 1986 An examination of the NR complement in different organs of a number of siblings originating from a cross involving transposon Mu-containing parents and having different levels of leaf NADH NR activity shows that the leaf NADH NR activity content and the scutellum NAD(P)H NR activity content are relatively independent of each other, indicating that the genetic programs specifying the NR content of these organs are not tightly coupled, if at all. NAD 184-188 nitrate reductase [NADH] 1 Zea mays 189-191 16665054-10 1986 An examination of the NR complement in different organs of a number of siblings originating from a cross involving transposon Mu-containing parents and having different levels of leaf NADH NR activity shows that the leaf NADH NR activity content and the scutellum NAD(P)H NR activity content are relatively independent of each other, indicating that the genetic programs specifying the NR content of these organs are not tightly coupled, if at all. NAD 184-188 nitrate reductase [NADH] 1 Zea mays 189-191 16665054-10 1986 An examination of the NR complement in different organs of a number of siblings originating from a cross involving transposon Mu-containing parents and having different levels of leaf NADH NR activity shows that the leaf NADH NR activity content and the scutellum NAD(P)H NR activity content are relatively independent of each other, indicating that the genetic programs specifying the NR content of these organs are not tightly coupled, if at all. NAD 221-225 nitrate reductase [NADH] 1 Zea mays 22-24 3015963-0 1986 Functional domains of assimilatory NADH:nitrate reductase from Chlorella. NAD 35-39 nitrate reductase [NADH] 1 Zea mays 40-57 3015963-2 1986 Besides the reduction of nitrate by NADH, nitrate reductase also catalyzes the partial activities NADH:cytochrome c reductase, NADH:ferricyanide reductase, and reduced methyl viologen:nitrate reductase. NAD 36-40 nitrate reductase [NADH] 1 Zea mays 42-59 3015963-2 1986 Besides the reduction of nitrate by NADH, nitrate reductase also catalyzes the partial activities NADH:cytochrome c reductase, NADH:ferricyanide reductase, and reduced methyl viologen:nitrate reductase. NAD 36-40 nitrate reductase [NADH] 1 Zea mays 184-201 3015963-2 1986 Besides the reduction of nitrate by NADH, nitrate reductase also catalyzes the partial activities NADH:cytochrome c reductase, NADH:ferricyanide reductase, and reduced methyl viologen:nitrate reductase. NAD 98-102 nitrate reductase [NADH] 1 Zea mays 42-59 3015963-2 1986 Besides the reduction of nitrate by NADH, nitrate reductase also catalyzes the partial activities NADH:cytochrome c reductase, NADH:ferricyanide reductase, and reduced methyl viologen:nitrate reductase. NAD 98-102 nitrate reductase [NADH] 1 Zea mays 184-201 3015963-8 1986 These results are consistent with a structure-function model of nitrate reductase which has the following features: FAD/NADH-binding domains exposed on the surface of the molecule, a protease-sensitive hinge region which connects the nitrate-reducing and NADH dehydrogenase moieties, and the quaternary structure maintained via association sites on the heme/molybdenum domain. NAD 120-124 nitrate reductase [NADH] 1 Zea mays 64-81 16667152-3 1989 NADH:nitrate reductase activity and enzyme protein, as measured with an enzyme-linked immunosorbent assay, increased in parallel during the 8 h nitrate treatment in air, but in O(2) the levels of enzyme activity and protein were depressed. NAD 0-4 nitrate reductase [NADH] 1 Zea mays 5-22 16667152-4 1989 NADH:nitrate reductase mRNA levels were the same in the air-and O(2)-treated leaves. NAD 0-4 nitrate reductase [NADH] 1 Zea mays 5-22 16666879-0 1989 cDNA Clones for Corn Leaf NADH:Nitrate Reductase and Chloroplast NAD(P):Glyceraldehyde-3-Phosphate Dehydrogenase : Characterization of the Clones and Analysis of the Expression of the Genes in Leaves as Influenced by Nitrate in the Light and Dark. NAD 26-30 nitrate reductase [NADH] 1 Zea mays 31-48 16666879-3 1989 The deduced amino acid sequence of Zmnrl was nearly identical to peptide sequences of corn leaf NADH:nitrate reductase. NAD 96-100 nitrate reductase [NADH] 1 Zea mays 101-118 16665101-6 1986 These results were taken to indicate that bromphenol blue and NADH donated electrons to nitrate reductase at different sites. NAD 62-66 nitrate reductase [NADH] 1 Zea mays 88-105 16665101-7 1986 When monoclonal antibodies prepared against corn and squash nitrate reductases were used to inhibit the nitrate reductase activities supported by NADH, bromphenol blue, and methyl viologen, differential inhibition was found which tended to indicate that the three electron donors were interacting with the enzyme at different sites. NAD 146-150 nitrate reductase [NADH] 1 Zea mays 60-77 16664640-9 1986 Western blots of polyacrylamide gels of native and denatured crude extracts showed that NADH:NR polypeptide was absent prior to treatment with N nutrients, but appeared after nitrate was given in dark or light. NAD 88-92 nitrate reductase [NADH] 1 Zea mays 93-95 16661130-12 1980 Inactivation of corn leaf NR by rice inactivator was inhibited by the simultaneous addition of NADH, but rice inactivator-inactivated corn leaf NR could not be reactivated by NADH. NAD 95-99 nitrate reductase [NADH] 1 Zea mays 26-28 16658530-3 1973 Activity of the root and scutella nitrate reductase was obtained with either NADH or NADPH, but that of the root enzyme with NADPH was only demonstrated in the absence of phosphate.Before leaf expansion, the nitrate reductase in the maize seedling was mainly in the scutellum. NAD 77-81 nitrate reductase [NADH] 1 Zea mays 34-51 235300-10 1975 The maize nitrate reductase, when partially inactivated by NADH and cyanide, was not altered as a substrate for the inactivating enzyme. NAD 59-63 nitrate reductase [NADH] 1 Zea mays 10-27 235300-11 1975 The maize root inactivating enzyme was also shown to inactivate the nitrate reductase (NADH) in the pea leaf. NAD 87-91 nitrate reductase [NADH] 1 Zea mays 68-85 16656864-1 1968 With respect to cofactor requirements, NADH, and FMNH(2) were equally effective as electron donors for nitrate reductase obtained from leaves of maize, marrow, and spinach, when the cofactors were supplied in optimal concentrations. NAD 39-43 nitrate reductase [NADH] 1 Zea mays 103-120 16656864-5 1968 Unity of NADH to FMNH(2) activities were obtained during: A) purification procedures (4 step, 30-fold); B) induction of nitrate reductase in corn seedlings with nitrate; and C) inactivation of nitrate reductase in intact or excised corn seedlings. NAD 9-13 nitrate reductase [NADH] 1 Zea mays 120-137 16656864-5 1968 Unity of NADH to FMNH(2) activities were obtained during: A) purification procedures (4 step, 30-fold); B) induction of nitrate reductase in corn seedlings with nitrate; and C) inactivation of nitrate reductase in intact or excised corn seedlings. NAD 9-13 nitrate reductase [NADH] 1 Zea mays 193-210 16656864-6 1968 The NADH- and FMNH(2)-dependent activities were not additive.A half-life for nitrate reductase of approximately 4 hours was estimated from the inactivation studies with excised corn seedlings. NAD 4-8 nitrate reductase [NADH] 1 Zea mays 77-94 16656864-8 1968 This was verified by reactivation with exogenous cysteine.Based on these current findings, and previous work, it is concluded that nitrate reductase is a single moiety with the ability to utilize either NADH or FMNH(2) as cofactor. NAD 203-207 nitrate reductase [NADH] 1 Zea mays 131-148 16656864-9 1968 However the high concentration of FMNH(2) required for optimal activity suggests that in vivo NADH is the electron donor and that nitrate reductase in higher plants should be designated NADH:nitrate reductase (E.C. NAD 94-98 nitrate reductase [NADH] 1 Zea mays 191-208 16656864-9 1968 However the high concentration of FMNH(2) required for optimal activity suggests that in vivo NADH is the electron donor and that nitrate reductase in higher plants should be designated NADH:nitrate reductase (E.C. NAD 186-190 nitrate reductase [NADH] 1 Zea mays 130-147 16656864-9 1968 However the high concentration of FMNH(2) required for optimal activity suggests that in vivo NADH is the electron donor and that nitrate reductase in higher plants should be designated NADH:nitrate reductase (E.C. NAD 186-190 nitrate reductase [NADH] 1 Zea mays 191-208