PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 11537374-1 1989 The gamma-irradiation of 0.1 M, O2-free, aqueous HCN was studied in the presence of ferrocyanide or ferricyanide in the concentration range 10(-3) - 10(-5) M. This study was carried out in order to get an insight into the possible role that cyanocomplexes of iron may have played in promoting prebiotic syntheses via the free-radical oligomerization of HCN. hexacyanoferrate II 84-96 metastasis associated lung adenocarcinoma transcript 1 Homo sapiens 49-52 2992572-5 1985 The rate of cytochrome c reduction is accelerated to 0.105 +/- 0.021 mu equiv min-1 (mg of protein)-1 when cytochrome c is pretreated with equimolar ferrocyanide. hexacyanoferrate II 149-161 cytochrome c, somatic Homo sapiens 12-24 2992389-0 1985 Characterization of cucumber ascorbate oxidase and its reaction with hexacyanoferrate (II). hexacyanoferrate II 69-85 L-ascorbate oxidase Cucumis sativus 29-46 2992389-4 1985 The reduction of AOase with a large excess of hexacyanoferrate(II) results in a selective reduction of the type-2 Cu, giving rise to an additional EPR-detectable species which is considered to be originated from partly reduced type-3 copper. hexacyanoferrate II 46-62 L-ascorbate oxidase Cucumis sativus 17-22 2992572-5 1985 The rate of cytochrome c reduction is accelerated to 0.105 +/- 0.021 mu equiv min-1 (mg of protein)-1 when cytochrome c is pretreated with equimolar ferrocyanide. hexacyanoferrate II 149-161 CD59 molecule (CD59 blood group) Homo sapiens 78-101 2992572-5 1985 The rate of cytochrome c reduction is accelerated to 0.105 +/- 0.021 mu equiv min-1 (mg of protein)-1 when cytochrome c is pretreated with equimolar ferrocyanide. hexacyanoferrate II 149-161 cytochrome c, somatic Homo sapiens 107-119 2992572-7 1985 The ferrocyanide-stimulated rate of cytochrome c reduction is further accelerated by the protonophore carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone (FCCP), probably because FCCP dissipates the membrane potential generated by electron transfer. hexacyanoferrate II 4-16 cytochrome c, somatic Homo sapiens 36-48 6193086-7 1983 In this modified medium, Karnovsky"s cupric ferrocyanide becomes the sole precipitate at the enzymatic site and this provides fine localization of acetylcholinesterase activity. hexacyanoferrate II 44-56 acetylcholinesterase (Cartwright blood group) Homo sapiens 147-167 2983756-9 1985 The chromaffin-vesicle electron-transfer system reduces cytochrome c relatively slowly, but the rate is greatly accelerated by low concentrations of ferrocyanide. hexacyanoferrate II 149-161 cytochrome c, somatic Homo sapiens 56-68 6995116-0 1980 Production of glycolate by oxidation of the 1,2-dihydroxyethyl-thamin-diphosphate intermediate of transketolase with hexacyanoferrate(III) or H2O2. hexacyanoferrate II 117-133 transketolase Homo sapiens 98-111 6284722-0 1982 Characterization of electron donation to cytochrome c-555 in Chromatium vinosum from ferrocyanide, tetramethylphenylenediamine and reduced dimethylquinone. hexacyanoferrate II 85-97 cytochrome c, somatic Homo sapiens 41-53 6284722-3 1982 The dependences of the reduction of ferricytochrome c-555 in the reaction center-cytochrome c complex on the redox potential and pH were investigated using N,N,N",N"-tetramethyl-p-phenylenediamine (TMPD), ferrocyanide, and reduced 2,5-dimethyl-p-quinone as electron donors. hexacyanoferrate II 205-217 cytochrome c, somatic Homo sapiens 41-53 6284722-7 1982 Ferrocyanide reduced cytochrome c-555 slowly with a rate constant of 7.8 X 10(3) M-1.s-1 at infinite salt concentration. hexacyanoferrate II 0-12 cytochrome c, somatic Homo sapiens 21-33 6292175-5 1982 Addition of ferrocyanide to intact cytochrome c-depleted mitochondria does not reduce cytochrome c1; treatment with N,N,N",N"-tetramethylphenylenediamine, Triton X-100, or sonic oscillation results in 30% reduction of cytochromes c + c1. hexacyanoferrate II 12-24 cytochrome c, somatic Homo sapiens 35-47 6268746-1 1981 Use of rigorous equilibration kinetics to evaluate rate constants for the Fe(CN)6 4- reduction of horse-heart cytochrome c in the oxidized form, cyt c (III), has shown that limiting kinetics do not apply with concentrations of Fe(CN)6 4- (the reactant in excess) in the range 2-10 x 10(-4) M, I = 0.10 M (NaCl). hexacyanoferrate II 74-83 cytochrome c, somatic Equus caballus 110-122 6995116-1 1980 In the presence of hexacyanoferrate(III), or other suitable oxidants, transketolase catalyzes the oxidative cleavage of its donor substrates xylulose 5-phosphate or fructose 6-phosphate into glycolate and glyceraldehyde 3-phosphate or erythrose 4-phosphate, respectively. hexacyanoferrate II 19-35 transketolase Homo sapiens 70-83 227900-1 1979 The kinetics of the oxidation-reduction reactions between horse heart cytochrome c, Euglena gracilis cytochrome c552, and ions (ascorbate, ferricyanide, and ferrocyanide) was investigated as a function of ionic strength at pH 7, 25 degrees C. The ionic strength was varied between 0.002 and 0.02 M. Data were analyzed according to four different functions of ionic strength. hexacyanoferrate II 157-169 cytochrome c, somatic Equus caballus 70-82 195599-2 1977 Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide. hexacyanoferrate II 78-90 cytochrome c, somatic Equus caballus 29-41 7378421-1 1980 The alternative electron donors ferrocyanide and hydroquinone have been shown to also act as inhibitors of dopamine-beta-hydroxylase (3,4-dihydroxyphenylethylamine, ascorbate:oxygen oxidoreductase (beta-hydroxylating), EC 1.14.17.1). hexacyanoferrate II 32-44 dopamine beta-hydroxylase Homo sapiens 107-132 7378421-8 1980 The potency of inhibition of dopamine-beta-hydroxylase by both ferrocyanide and hydroquinone is dependent on the degree of protonation of a group in the enzyme having a pKa of 5.3. hexacyanoferrate II 63-75 dopamine beta-hydroxylase Homo sapiens 29-54 223635-3 1979 In the absence of cytochrome c, ferrocyanide or ferrous sulphate reduces cytochrome c oxidase (EC 1.9.3.1), but no continuous oxygen uptake ensues, as it does with N,N,N",N"-tetramethyl-p-phenylenediamine or reduced phenazine methosulphate as reductants, unless a substoichiometric amount of cytochrome c or an excess of clupein is present. hexacyanoferrate II 32-44 cytochrome c, somatic Homo sapiens 73-85 223635-3 1979 In the absence of cytochrome c, ferrocyanide or ferrous sulphate reduces cytochrome c oxidase (EC 1.9.3.1), but no continuous oxygen uptake ensues, as it does with N,N,N",N"-tetramethyl-p-phenylenediamine or reduced phenazine methosulphate as reductants, unless a substoichiometric amount of cytochrome c or an excess of clupein is present. hexacyanoferrate II 32-44 cytochrome c, somatic Homo sapiens 73-85 223635-6 1979 Cytochrome c, porphyrin cytochrome c and clupein all stimulate the reduction of cytochrome aa3 by ferrocyanide. hexacyanoferrate II 98-110 cytochrome c, somatic Homo sapiens 0-12 223635-6 1979 Cytochrome c, porphyrin cytochrome c and clupein all stimulate the reduction of cytochrome aa3 by ferrocyanide. hexacyanoferrate II 98-110 cytochrome c, somatic Homo sapiens 24-36 157102-0 1979 Novel pronounced reversible inhibition of phosphofructokinase, glucose 6-phosphate dehydrogenase, and phosphoglucose isomerase by hexacyanoferrate (II). hexacyanoferrate II 130-146 glucose-6-phosphate dehydrogenase Homo sapiens 63-96 157102-0 1979 Novel pronounced reversible inhibition of phosphofructokinase, glucose 6-phosphate dehydrogenase, and phosphoglucose isomerase by hexacyanoferrate (II). hexacyanoferrate II 130-146 glucose-6-phosphate isomerase Homo sapiens 102-126 447731-8 1979 An equimolar amount of cytochrome b5 was more effective than ferrocyanide in the enzymatic reduction of metmyoglobin. hexacyanoferrate II 61-73 cytochrome b5 type A Bos taurus 23-36 448060-0 1979 Ferrocyanide staining of transferrin and ferritin-conjugated antibody to transferrin. hexacyanoferrate II 0-12 transferrin Mus musculus 25-36 448060-0 1979 Ferrocyanide staining of transferrin and ferritin-conjugated antibody to transferrin. hexacyanoferrate II 0-12 transferrin Mus musculus 73-84 16660377-1 1978 The 4S cytochrome c (Cyt c) reductase activity of several plant species was markedly stimulated by cyanide and ferrocyanide but those of the 8S nitrate reductase component and other particulate components of the maize (Zea mays L.) scutellum by comparison, were increased only slightly. hexacyanoferrate II 111-123 cytochrome c Zea mays 7-19 16660377-1 1978 The 4S cytochrome c (Cyt c) reductase activity of several plant species was markedly stimulated by cyanide and ferrocyanide but those of the 8S nitrate reductase component and other particulate components of the maize (Zea mays L.) scutellum by comparison, were increased only slightly. hexacyanoferrate II 111-123 cytochrome c Zea mays 21-26 16660377-2 1978 The effect of cyanide and ferrocyanide was not due to elimination of cytochrome oxidase interference but resulted from the stimulation of NADH-dependent reduction of Cyt c. hexacyanoferrate II 26-38 cytochrome c Zea mays 166-171 16660377-3 1978 A 4S Cyt c reductase component which could be isolated by ammonium sulfate fractionation and diethyl-aminoethyl-cellulose chromatography was found to be stimulated markedly by cyanide and ferrocyanide. hexacyanoferrate II 188-200 cytochrome c Zea mays 5-10 195599-2 1977 Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide. hexacyanoferrate II 78-90 cytochrome c, somatic Equus caballus 62-74 32460478-6 2020 Among the investigated anions, the low-valent anions showed no impact on the ICR direction, while the high-valent component ferrocyanide [Fe(CN)64-] caused significant ICR inversion. hexacyanoferrate II 124-136 general transcription factor IIE subunit 1 Homo sapiens 138-146 776982-0 1976 Oxidation of the carbanion intermediate of transaldolase by hexacyanoferrate (III). hexacyanoferrate II 60-76 transaldolase 1 Homo sapiens 43-56 776982-1 1976 The transaldolase-dihydroxyacetone carbanion intermediate formed in the reaction of transaldolase with its donor substrates fructose-6-P or sedoheptulose-7-P is susceptible to oxidation by hexacyanoferrate(III). hexacyanoferrate II 189-205 transaldolase 1 Homo sapiens 4-17 776982-1 1976 The transaldolase-dihydroxyacetone carbanion intermediate formed in the reaction of transaldolase with its donor substrates fructose-6-P or sedoheptulose-7-P is susceptible to oxidation by hexacyanoferrate(III). hexacyanoferrate II 189-205 transaldolase 1 Homo sapiens 84-97 776982-4 1976 In the presence of hexacyanoferrate(III) transaldolase thus functions as an efficient catalyst of the oxidative cleavage of its donor substrates fructose-6-P or sedoheptulose-7-P into hydroxypyruvaldehyde and glyceraldehyde-3-P or erythrose-4-P, respectively. hexacyanoferrate II 19-35 transaldolase 1 Homo sapiens 41-54 5116561-8 1971 The peroxide compound of yeast cytochrome c peroxidase was found to have two oxidizing equivalents accessible to cytochrome c but only one readily accessible to ferrocyanide. hexacyanoferrate II 161-173 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 31-54 4172645-0 1967 A thiocholine-lead ferrocyanide method for acetylcholinesterase. hexacyanoferrate II 19-31 acetylcholinesterase (Cartwright blood group) Homo sapiens 43-63 33603152-4 2021 With use of an empirical rule of the frequencies of the CN- stretching mode in ferrocyanide ([FeII(CN)6]4-) and ferricyanide ([FeIII(CN)6]3-), the oxidation processes of Co-PBAs were determined against the Fe concentration (y) and temperature (T). hexacyanoferrate II 79-91 general transcription factor IIE subunit 1 Homo sapiens 94-96 33151212-1 2020 Prebiotically plausible ferrocyanide-ferricyanide photoredox cycling oxidatively converts thiourea to cyanamide, whilst HCN is reductively homologated to intermediates which either react directly with the cyanamide giving 2-aminoazoles, or have the potential to do so upon loss of HCN from the system. hexacyanoferrate II 24-36 metastasis associated lung adenocarcinoma transcript 1 Homo sapiens 120-123 33151212-1 2020 Prebiotically plausible ferrocyanide-ferricyanide photoredox cycling oxidatively converts thiourea to cyanamide, whilst HCN is reductively homologated to intermediates which either react directly with the cyanamide giving 2-aminoazoles, or have the potential to do so upon loss of HCN from the system. hexacyanoferrate II 24-36 metastasis associated lung adenocarcinoma transcript 1 Homo sapiens 281-284 10021-9 1975 Ferrocyanide reduction of ferri-horse heart cytochrome c takes place in a kinetically complex manner. hexacyanoferrate II 0-12 cytochrome c, somatic Equus caballus 44-56 4368557-0 1974 Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. hexacyanoferrate II 47-59 cytochrome c, somatic Homo sapiens 0-12 4368558-0 1974 Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. hexacyanoferrate II 47-59 cytochrome c, somatic Homo sapiens 0-12 32545422-7 2020 The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. hexacyanoferrate II 141-157 fibrinogen beta chain Homo sapiens 16-26 32215420-2 2020 Here, we report the use of hexacyanoferrate(ii) and hexacyanoferrate(iii) as electroactive crosslinking agents for the formation of nanometer-sized redox-active polyamine-redox-salt aggregates (rPSA) in bulk suspension. hexacyanoferrate II 27-43 aminopeptidase puromycin sensitive Rattus norvegicus 194-198 32215420-2 2020 Here, we report the use of hexacyanoferrate(ii) and hexacyanoferrate(iii) as electroactive crosslinking agents for the formation of nanometer-sized redox-active polyamine-redox-salt aggregates (rPSA) in bulk suspension. hexacyanoferrate II 52-68 aminopeptidase puromycin sensitive Rattus norvegicus 194-198 31713687-10 2019 Abeta(1-42) capturing by the peptide led to repulsion of ferrocyanide/ferricyanide redox couple. hexacyanoferrate II 57-69 amyloid beta precursor protein Homo sapiens 0-5 31864626-4 2020 The proposed protocols were conducted by using the model oxidoreductases of glucose oxidase (GOx) and the enzyme cascade of lactate dehydrogenase (LDH)/diaphorase to catalytically convert ferricyanide to ferrocyanide, which switched on fluorescence of the detection systems. hexacyanoferrate II 204-216 hydroxyacid oxidase 1 Homo sapiens 76-91 31864626-4 2020 The proposed protocols were conducted by using the model oxidoreductases of glucose oxidase (GOx) and the enzyme cascade of lactate dehydrogenase (LDH)/diaphorase to catalytically convert ferricyanide to ferrocyanide, which switched on fluorescence of the detection systems. hexacyanoferrate II 204-216 hydroxyacid oxidase 1 Homo sapiens 93-96 30831419-5 2019 The interaction of the CRH with the recognition layer of the immobilized half-antibody on the nanostructured surface was carried out by incubation at 4 C for 2 h. A dissolution of [Fe(CN)6]4-/[Fe(CN)6]3- as a redox probe was used to study the electrochemical responses of the nanostructured surface and the immobilization processes of the half-antibody and detection of CRH, using cyclic voltammetry and electrochemical impedance spectroscopy. hexacyanoferrate II 182-191 corticotropin releasing hormone Homo sapiens 23-26 31243577-5 2019 If the CRP on the paper device is contacted with Ca (II) ions, the current (measured by using hexacyanoferrate as the electrochemical probe) decreases. hexacyanoferrate II 94-110 C-reactive protein Homo sapiens 7-10 31243577-5 2019 If the CRP on the paper device is contacted with Ca (II) ions, the current (measured by using hexacyanoferrate as the electrochemical probe) decreases. hexacyanoferrate II 94-110 carbonic anhydrase 2 Homo sapiens 49-56 23999654-3 2013 In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs. hexacyanoferrate II 264-280 phenylalanine hydroxylase Homo sapiens 55-58 30732787-5 2019 Co(II)-chelated CEC cryogels have been used for fabrication of Co(II) ferrocyanide-containing composite with the distribution coefficient for 137Cs of 140,000 ml/g and the adsorption capacity of ~1 mmol/g. hexacyanoferrate II 70-82 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-5 30732787-5 2019 Co(II)-chelated CEC cryogels have been used for fabrication of Co(II) ferrocyanide-containing composite with the distribution coefficient for 137Cs of 140,000 ml/g and the adsorption capacity of ~1 mmol/g. hexacyanoferrate II 70-82 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 30712159-6 2019 CRP was quantified by measuring the changes in the charge-transfer resistance of the electrode by using hexacyanoferrate as the redox probe. hexacyanoferrate II 104-120 C-reactive protein Homo sapiens 0-3 29594452-7 2018 Hexacyanoferrate was used as an electrochemical probe to study the dependence of the peak current on lysozyme concentration. hexacyanoferrate II 0-16 lysozyme Homo sapiens 101-109 29594452-14 2018 The changes of peak current for the electrochemical probe hexacyanoferrate (Fe(CN)63-/4-) in the presence and absence of lysozyme was traced. hexacyanoferrate II 58-74 lysozyme Homo sapiens 121-129 29594654-0 2018 Aptamer-based determination of tumor necrosis factor alpha using a screen-printed graphite electrode modified with gold hexacyanoferrate. hexacyanoferrate II 120-136 tumor necrosis factor Homo sapiens 31-58 27973360-2 2016 This paper deals with the degradation of acid red-26 (AR-26), an azo dye by hexacyanoferrate (abbreviated as HCF) (III) using iridium nanoparticles. hexacyanoferrate II 76-92 host cell factor C1 Homo sapiens 109-112 26588324-6 2015 The specific interaction of CRP with phosphorylcholine in a calcium-containing buffer solution was determined by differential pulse voltammetry, which measures the altered redox reaction between the indicators ferricyanide/ferrocyanide as a result of the binding event. hexacyanoferrate II 223-235 C-reactive protein Homo sapiens 28-31 26343443-1 2015 We present a novel electrochemical glucose sensor employing an interdigitated array (IDA) of 1:1 aspect ratio carbon nanoelectrodes for the electrochemical-enzymatic redox cycling of redox species (ferricyanide/ferrocyanide) between glucose oxidase (GOx) and the two comb-shaped nanoelectrodes of the IDA. hexacyanoferrate II 211-223 hydroxyacid oxidase 1 Homo sapiens 233-248 26343443-1 2015 We present a novel electrochemical glucose sensor employing an interdigitated array (IDA) of 1:1 aspect ratio carbon nanoelectrodes for the electrochemical-enzymatic redox cycling of redox species (ferricyanide/ferrocyanide) between glucose oxidase (GOx) and the two comb-shaped nanoelectrodes of the IDA. hexacyanoferrate II 211-223 hydroxyacid oxidase 1 Homo sapiens 250-253 25127647-6 2014 At a higher menadione concentration (100 muM), the ferrocyanide generation rate decreased within 30 min because of the cytotoxic effect of menadione. hexacyanoferrate II 51-63 latexin Homo sapiens 41-44 30431259-7 2018 Finally, we show that the exposed interface between sp2 and sp3 carbon layers (i.e. the laser-ablated diamond surface) revealed faster kinetics than the untreated BDD in both ferrocyanide and RuHex mediators, which can be used for electrochemical (bio)sensing. hexacyanoferrate II 175-187 Sp2 transcription factor Homo sapiens 52-55 30431259-7 2018 Finally, we show that the exposed interface between sp2 and sp3 carbon layers (i.e. the laser-ablated diamond surface) revealed faster kinetics than the untreated BDD in both ferrocyanide and RuHex mediators, which can be used for electrochemical (bio)sensing. hexacyanoferrate II 175-187 Sp3 transcription factor Homo sapiens 60-63 30101890-7 2018 Thus, epsilonPL is considered to be a useful additive for glucose sensors based on the [Fe(CN)6]4-/3--mediated GOx catalytic current. hexacyanoferrate II 88-97 hydroxyacid oxidase 1 Homo sapiens 111-114 29018930-4 2017 Under the optimal experimental conditions, the DPV peak currents of hexacyanoferrate/hexacyanoferrite changed linearly with Gly concentration in the range from 5 to 800 ng mL-1, with a detection limit of 0.27 ng mL-1 (S/N = 3). hexacyanoferrate II 68-84 L1 cell adhesion molecule Mus musculus 172-176 29018930-4 2017 Under the optimal experimental conditions, the DPV peak currents of hexacyanoferrate/hexacyanoferrite changed linearly with Gly concentration in the range from 5 to 800 ng mL-1, with a detection limit of 0.27 ng mL-1 (S/N = 3). hexacyanoferrate II 68-84 L1 cell adhesion molecule Mus musculus 212-216 28671628-3 2017 In addition, the effect of the ferrocyanide concentration on the SWASV detection of Cd2+ in the presence of Cu2+ was investigated. hexacyanoferrate II 31-43 CD2 molecule Homo sapiens 84-87 27607732-2 2016 Herein we demonstrate for the first time the liberation of CH4 and NH3 from a well-defined iron cyanide coordination complex, [SiP(iPr) 3 ]Fe(CN) (where [SiP(iPr) 3 ] represents a tris(phosphine)silyl ligand), on exposure to proton and electron equivalents. hexacyanoferrate II 91-103 tumor protein p53 inducible nuclear protein 1 Homo sapiens 127-137 27607732-2 2016 Herein we demonstrate for the first time the liberation of CH4 and NH3 from a well-defined iron cyanide coordination complex, [SiP(iPr) 3 ]Fe(CN) (where [SiP(iPr) 3 ] represents a tris(phosphine)silyl ligand), on exposure to proton and electron equivalents. hexacyanoferrate II 91-103 tumor protein p53 inducible nuclear protein 1 Homo sapiens 154-164 25127647-4 2014 Generation of ferrocyanide was observed immediately after the addition of a lower concentration (10 muM) of menadione. hexacyanoferrate II 14-26 latexin Homo sapiens 100-103 24296061-2 2014 The biotinylated aptamer of thrombin was immobilized onto an avidin-graphite epoxy composite (AvGEC) electrode surface by affinity interaction between biotin and avidin; electrochemical impedance measurements were performed in a solution containing the redox marker ferrocyanide/ferricyanide. hexacyanoferrate II 266-278 coagulation factor II, thrombin Homo sapiens 28-36 24437480-3 2014 Cyclic voltammetry displays a reversible peak with E(1/2) at -1.04 V vs ferrocyanide attributed to the (Co(III/II)TCPP)CoPIZA redox couple and a quasi-reversible peak at -1.45 V vs ferrocyanide, which corresponds to the reduction of (Co(II/I)TCPP)CoPIZA. hexacyanoferrate II 72-84 mitochondrially encoded cytochrome c oxidase III Homo sapiens 107-110 23999654-3 2013 In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs. hexacyanoferrate II 264-280 phenylalanine hydroxylase Homo sapiens 75-78 22294389-4 2012 CDH induces PB formation via both reduction of ferricyanide to ferrocyanide reacting with an excess of Fe3+ (pathway 1) and reduction of ferric ions to Fe2+ reacting with the excess of ferricyanide (pathway 2). hexacyanoferrate II 63-75 choline dehydrogenase Homo sapiens 0-3 23780697-3 2013 However, in the presence of iron, the HCN was captured in the form of a ferrocyanide, partially inhibiting the formation of amino acids. hexacyanoferrate II 72-84 metastasis associated lung adenocarcinoma transcript 1 Homo sapiens 38-41 22101009-8 2012 A simple kinetic model of NO autoxidation is able to explain the extent of cytochrome c oxidation assuming a rate constant of 3x10(6)M(-1)s(-1) for the reaction of NO(2)( ) with ferrocytochrome c. The importance of NO(2)( ) was confirmed by the addition of scavengers such as urate and ferrocyanide. hexacyanoferrate II 286-298 cytochrome c, somatic Homo sapiens 75-87 22177076-4 2012 In electrochemical biosensors, interactions between the immobilized kappa-CN molecules and chymosin (the active component of rennet) were studied by performing cyclic voltammetry, differential pulsed voltammetry, and electrochemical impedance spectroscopy (EIS) measurements, using hexacyanoferrate(II)/(III) couple as a redox probe. hexacyanoferrate II 282-298 casein kappa Homo sapiens 68-76 22666416-5 2012 Based on ferrocyanide quenching, fluorescence polarization, quantum yield values and viscosity results a strong intercalative binding of BC1 and BC2 to the RNA triplex has been demonstrated. hexacyanoferrate II 9-21 charged multivesicular body protein 2A Homo sapiens 145-148 22132924-10 2011 The CSF flow pathway was traced by staining the ferritin with ferrocyanide. hexacyanoferrate II 62-74 colony stimulating factor 2 Rattus norvegicus 4-7 17205271-4 2007 Electrochemical impedance spectroscopy (EIS) of ferrocyanide followed the assembly process and verified the successful immobilization of IO(4)(-) - GOx on ASNPs modified on gold electrodes. hexacyanoferrate II 48-60 hydroxyacid oxidase 1 Homo sapiens 148-151 21073422-0 2010 Inhibition of transketolase by hexacyanoferrate(III). hexacyanoferrate II 31-47 transketolase Homo sapiens 14-27 21073422-1 2010 The effect of hexacyanoferrate(III) on the catalytic activity of transketolase has been studied. hexacyanoferrate II 14-30 transketolase Homo sapiens 65-78 19456182-4 2009 In neutral electrolytes, the LS1- and LS2-modified electrodes behaved as anionic coatings, showing an increase in the charge transfer resistance (R(ct)) for the ferrocyanide/ferricyanide redox couple. hexacyanoferrate II 161-173 serpin family D member 1 Homo sapiens 38-41 19123805-5 2009 Films constituted by more than nine PSS/PAH bilayers are still permeable to hexacyanoferrate(II) ions, Fe(CN)(6)4-, whatever the nature of the supporting salt anion. hexacyanoferrate II 76-92 PSS Homo sapiens 36-39 19123805-5 2009 Films constituted by more than nine PSS/PAH bilayers are still permeable to hexacyanoferrate(II) ions, Fe(CN)(6)4-, whatever the nature of the supporting salt anion. hexacyanoferrate II 76-92 phenylalanine hydroxylase Homo sapiens 40-43 18755579-7 2008 Binding of thrombin to an aptamer has also been detected using the ferricyanide/ferrocyanide redox couple as electrochemical indicator. hexacyanoferrate II 80-92 coagulation factor II, thrombin Homo sapiens 11-19 17203264-4 2007 NADH is converted to NAD+ by applying hexacyanoferrate(III) as oxidant in the presence of DI. hexacyanoferrate II 38-54 dihydrolipoamide dehydrogenase Homo sapiens 90-92 21035664-4 2010 In addition, the electrocatalytic behavior of this modified electrode was exploited as a sensitive detection system for the reduction of RDX high explosive, hydrogen peroxide and hexacyanoferrate (HCF) by cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS) techniques. hexacyanoferrate II 197-200 radixin Homo sapiens 137-140 16618178-3 2006 Approach curves were recorded with ferrocyanide as a mediator at different coverages of cytochrome c and at different substrate potentials, allowing the measurement of k(BI) = 2 x 10(8) mol(-1) cm3 s(-1) for the bimolecular ET and k degrees = 15 s(-1) for the tunneling ET. hexacyanoferrate II 35-47 cytochrome c, somatic Homo sapiens 88-100 15780631-8 2005 The best hCA IV inhibitors were dicyanocuprate (K(I) of 9.8 microM) and hexacyanoferrate(II) (K(I) of 10.0 microM), whereas the worst ones were tetrafluoroborate and hexafluoroaluminate (K(I)s in the range of 124-126 mM). hexacyanoferrate II 72-88 carbonic anhydrase 4 Homo sapiens 9-15 16018892-1 2005 Upon exposure to ultraviolet (UV) radiation, non-toxic hexacyanoferrate (II) (Fe(CN)6(-4)) undergoes direct photolysis, resulting in the liberation of toxic free cyanide (HCN,CN-). hexacyanoferrate II 55-71 metastasis associated lung adenocarcinoma transcript 1 Homo sapiens 171-174 15807618-3 2005 However, the contact of this film with a poly(allylamine) (PAH) or a poly(L-glutamic acid) (PGA) solution leads to the release of ferrocyanide ions from the multilayer. hexacyanoferrate II 130-142 phenylalanine hydroxylase Homo sapiens 59-62 15807618-6 2005 When the film is then brought in contact with a PAH solution, the PAH chains from the solution are expected to strongly interact with the ferrocyanide ions and thus induce a diffusion mechanism of the multivalent anions out of the film, the film/solution interface playing the role of a sink for these ions. hexacyanoferrate II 138-150 phenylalanine hydroxylase Homo sapiens 48-51 15807618-6 2005 When the film is then brought in contact with a PAH solution, the PAH chains from the solution are expected to strongly interact with the ferrocyanide ions and thus induce a diffusion mechanism of the multivalent anions out of the film, the film/solution interface playing the role of a sink for these ions. hexacyanoferrate II 138-150 phenylalanine hydroxylase Homo sapiens 66-69 15780631-10 2005 The best hCA IX inhibitors were on the other hand cyanide, heptafluoroniobate and dicyanoargentate (K(I)s in the range of 4 microM-0.33 mM), whereas the worst ones were hexacyanoferrate(III) and hexacyanoferrate(II). hexacyanoferrate II 169-185 carbonic anhydrase 9 Homo sapiens 9-15 15780631-10 2005 The best hCA IX inhibitors were on the other hand cyanide, heptafluoroniobate and dicyanoargentate (K(I)s in the range of 4 microM-0.33 mM), whereas the worst ones were hexacyanoferrate(III) and hexacyanoferrate(II). hexacyanoferrate II 195-211 carbonic anhydrase 9 Homo sapiens 9-15 14999009-7 2004 The addition of ferrocyanide enhanced both the reduction rate and final reduction level of the diethylpyrocarbonate-treated cytochrome b(561) when ascorbate was used as a reductant. hexacyanoferrate II 16-28 cytochrome b Bos taurus 124-136 15449937-0 2004 Crystal structures of HbA2 and HbE and modeling of hemoglobin delta 4: interpretation of the thermal stability and the antisickling effect of HbA2 and identification of the ferrocyanide binding site in Hb. hexacyanoferrate II 173-185 hemoglobin subunit alpha 2 Homo sapiens 22-26 15449937-11 2004 The crystal structure of a ferrocyanide-bound HbA(2) at 1.88 A resolution is also presented here, which throws light on the location and the mode of binding of ferrocyanide anion with hemoglobin, predominantly using the residues involved in DPG binding. hexacyanoferrate II 27-39 hemoglobin subunit alpha 2 Homo sapiens 46-52 11570891-3 2001 Ferri/ferrocyanide can mediate reduction of DEPC-treated cytochrome b(561) by ascorbic acid, indicating that DEPC-inhibited cytochrome b(561) cannot accept electrons from a hydrogen-atom donor like ascorbate but can still accept electrons from an electron donor like ferrocyanide. hexacyanoferrate II 6-18 mitochondrially encoded cytochrome b Homo sapiens 57-69 12379149-7 2003 The anion-activated DBH was inhibited when assayed with ferrocyanide and activated when assayed with TMPD as electron donors by increasing the pH (5.1 to 6.0). hexacyanoferrate II 56-68 dopamine beta-hydroxylase Homo sapiens 20-23 14577762-1 2003 The dissociation of apoferritin into subunits at pH 2 followed by its re-formation at pH 8.5 in the presence of hexacyanoferrate(III) gave rise to a solution containing hexacyanoferrate(III) trapped within the apoferritin and hexacyanoferrate(III) outside it. hexacyanoferrate II 112-128 ferritin heavy chain 1 Homo sapiens 20-31 14577762-1 2003 The dissociation of apoferritin into subunits at pH 2 followed by its re-formation at pH 8.5 in the presence of hexacyanoferrate(III) gave rise to a solution containing hexacyanoferrate(III) trapped within the apoferritin and hexacyanoferrate(III) outside it. hexacyanoferrate II 112-128 ferritin heavy chain 1 Homo sapiens 210-221 14577762-1 2003 The dissociation of apoferritin into subunits at pH 2 followed by its re-formation at pH 8.5 in the presence of hexacyanoferrate(III) gave rise to a solution containing hexacyanoferrate(III) trapped within the apoferritin and hexacyanoferrate(III) outside it. hexacyanoferrate II 169-185 ferritin heavy chain 1 Homo sapiens 20-31 14577762-1 2003 The dissociation of apoferritin into subunits at pH 2 followed by its re-formation at pH 8.5 in the presence of hexacyanoferrate(III) gave rise to a solution containing hexacyanoferrate(III) trapped within the apoferritin and hexacyanoferrate(III) outside it. hexacyanoferrate II 169-185 ferritin heavy chain 1 Homo sapiens 210-221 14577762-1 2003 The dissociation of apoferritin into subunits at pH 2 followed by its re-formation at pH 8.5 in the presence of hexacyanoferrate(III) gave rise to a solution containing hexacyanoferrate(III) trapped within the apoferritin and hexacyanoferrate(III) outside it. hexacyanoferrate II 169-185 ferritin heavy chain 1 Homo sapiens 20-31 14577762-1 2003 The dissociation of apoferritin into subunits at pH 2 followed by its re-formation at pH 8.5 in the presence of hexacyanoferrate(III) gave rise to a solution containing hexacyanoferrate(III) trapped within the apoferritin and hexacyanoferrate(III) outside it. hexacyanoferrate II 169-185 ferritin heavy chain 1 Homo sapiens 210-221 16220934-1 2003 We developed a simple contrasting procedure to improve the AFM visualization of single positively charged polymer chains deposited on substrates of a relatively high roughness via the decoration of the molecules with hexacyanoferrate anions or negatively charged clusters of cyanide-bridged complexes. hexacyanoferrate II 217-233 afamin Homo sapiens 59-62 11570891-3 2001 Ferri/ferrocyanide can mediate reduction of DEPC-treated cytochrome b(561) by ascorbic acid, indicating that DEPC-inhibited cytochrome b(561) cannot accept electrons from a hydrogen-atom donor like ascorbate but can still accept electrons from an electron donor like ferrocyanide. hexacyanoferrate II 6-18 mitochondrially encoded cytochrome b Homo sapiens 124-136 11421701-1 2001 Radical salts of bis(ethylenethia)tetrathiafulvalene (BET-TTF) with the octahedral anions hexacyanoferrate(III) and nitroprusside. hexacyanoferrate II 90-106 delta/notch like EGF repeat containing Homo sapiens 54-57 11569835-1 2001 Limiting currents for the reduction of hexacyanoferrate-(III), i(lim), in aqueous solutions have been recorded in the presence of convective flow generated by a focused acoustic source with its main axis placed normal to the surface of a circular Au electrode embedded in a coplanar Teflon shroud. hexacyanoferrate II 39-55 PDZ and LIM domain 5 Homo sapiens 65-68 11421701-1 2001 Radical salts of bis(ethylenethia)tetrathiafulvalene (BET-TTF) with the octahedral anions hexacyanoferrate(III) and nitroprusside. hexacyanoferrate II 90-106 ras homolog family member H Homo sapiens 58-61 10502069-1 1999 We describe an improved copper ferrocyanide-based method for cytochemical detection of glucose-6-phosphate dehydrogenase (G6PD), which was used to localize the enzyme within the ultrastructure of rat hepatocytes and adrenocortical cells. hexacyanoferrate II 31-43 glucose-6-phosphate dehydrogenase Rattus norvegicus 87-120 10834943-3 2000 In the present study, ferrocyanide and thiols, which are susceptible to one-electron and two-electron oxidation, respectively, were subjected to a flux of superoxide in the presence and absence of SOD or SOD mimics. hexacyanoferrate II 22-34 superoxide dismutase 1 Homo sapiens 197-200 23604878-1 2001 The ultrastructural features of perikaryal mitochondria positive to the copper ferrocyanide cytochemical reaction due to SDH activity were investigated in Purkinje cells of adult rats fed a vitamin E (alpha-tocopherol) deficient diet (AVED) for 11 months. hexacyanoferrate II 79-91 serine dehydratase Rattus norvegicus 121-124 11005823-1 2000 The copper- and zinc-containing superoxide dismutase can catalyze the oxidation of ferrocyanide by O(2) as well as the reduction of ferricyanide by O(2). hexacyanoferrate II 83-95 superoxide dismutase 1 Homo sapiens 32-52 10502069-1 1999 We describe an improved copper ferrocyanide-based method for cytochemical detection of glucose-6-phosphate dehydrogenase (G6PD), which was used to localize the enzyme within the ultrastructure of rat hepatocytes and adrenocortical cells. hexacyanoferrate II 31-43 glucose-6-phosphate dehydrogenase Rattus norvegicus 122-126 1846158-4 1991 On the basis of oxidative polymerization of 3, 3"-diaminobenzidine by cytochrome oxidase (CYO) an cupric ferrocyanide deposition by monoamine oxidase (MAO), microcylinders were demonstrated to exhibit activity of these enzymes. hexacyanoferrate II 105-117 monoamine oxidase A Rattus norvegicus 132-149 9526032-0 1998 Ferrocyanide-peroxidase activity of cytochrome c oxidase Redox interaction of mitochondrial cytochrome c oxidase (COX) with ferrocyanide/ferricyanide couple is greatly accelerated by polycations, such as poly-l-lysine [Musatov et al. hexacyanoferrate II 124-136 cytochrome c, somatic Homo sapiens 36-48 9526032-0 1998 Ferrocyanide-peroxidase activity of cytochrome c oxidase Redox interaction of mitochondrial cytochrome c oxidase (COX) with ferrocyanide/ferricyanide couple is greatly accelerated by polycations, such as poly-l-lysine [Musatov et al. hexacyanoferrate II 124-136 cytochrome c, somatic Homo sapiens 92-104 8286338-9 1994 The fluorescence decrease with time paralleled the decrease in activity of H2O2-oxidized CCP using both ferrocytochrome c and ferrocyanide as substrates, indicating that tryptophan and activity loss occurred on similar time scales. hexacyanoferrate II 126-138 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 89-92 1552180-1 1992 We introduce a one-step histochemical method with cobalt as the precipitating agent for ferrocyanide for the light microscopic demonstration of acetylcholinesterase activity. hexacyanoferrate II 88-100 acetylcholinesterase (Cartwright blood group) Homo sapiens 144-164 18967368-3 1998 Some considerations regarding the current signals obtained from flow injection experiments using both a 5- and a 750-mum radius platinum electrode were carried out in order to achieve the lowest limit of detection, a value of 0.03 mumol dm(-3) ferrocyanide being calculated by using the 5-mum radius microelectrode as amperometric detector. hexacyanoferrate II 244-256 latexin Homo sapiens 117-120 18967368-3 1998 Some considerations regarding the current signals obtained from flow injection experiments using both a 5- and a 750-mum radius platinum electrode were carried out in order to achieve the lowest limit of detection, a value of 0.03 mumol dm(-3) ferrocyanide being calculated by using the 5-mum radius microelectrode as amperometric detector. hexacyanoferrate II 244-256 latexin Homo sapiens 231-234 1846158-4 1991 On the basis of oxidative polymerization of 3, 3"-diaminobenzidine by cytochrome oxidase (CYO) an cupric ferrocyanide deposition by monoamine oxidase (MAO), microcylinders were demonstrated to exhibit activity of these enzymes. hexacyanoferrate II 105-117 monoamine oxidase A Rattus norvegicus 151-154 2155024-8 1990 Acta 784, 189-191) reductants such as ascorbic acid and ferrocyanide convert Compound II, which accumulates during turnover, into active myeloperoxidase. hexacyanoferrate II 56-68 myeloperoxidase Homo sapiens 137-152 33773728-3 2021 Firstly, ascorbic acid, a product from ALP-catalyzed hydrolysis of 2-phospho-l-ascorbic acid (AAP), converted yellow ferricyanide into ferrocyanide. hexacyanoferrate II 135-147 alkaline phosphatase, placental Homo sapiens 39-42 33773728-3 2021 Firstly, ascorbic acid, a product from ALP-catalyzed hydrolysis of 2-phospho-l-ascorbic acid (AAP), converted yellow ferricyanide into ferrocyanide. hexacyanoferrate II 135-147 serpin family F member 2 Homo sapiens 94-97 34534004-6 2021 The adsorption of ferrocyanide onto kaolinite indicates an exothermic and outer-sphere interaction, which results in degeneracy breakdown for C N stretch energy into two new bands of FTIR-ATR spectrum. hexacyanoferrate II 18-30 ATR serine/threonine kinase Homo sapiens 190-193 34361764-0 2021 Composite Zn(II) Ferrocyanide/Polyethylenimine Cryogels for Point-of-Use Selective Removal of Cs-137 Radionuclides. hexacyanoferrate II 17-29 citrate synthase Homo sapiens 94-96 34764826-6 2021 In ferrocyanide medium, PSA detection as low as 3, 2.96, and 0.85 ng mL-1 was achieved with a dynamic range from 0.5 to 7 ng ml-1, in accord with clinical values, using cyclic voltammetry, square wave voltammetry, and electrochemical impedance spectroscopy, respectively. hexacyanoferrate II 3-15 kallikrein related peptidase 3 Homo sapiens 24-27