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Volumn 41, Issue 1, 2013, Pages 589-594
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Investigation of electrocatalytic pathway for hemoglobin toward nitric oxide by electrochemical approach based on protein controllable unfolding and in-situ reaction
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Author keywords
Electrochemistry; Hemoglobin; In situ reaction; Nitric oxide; Unfolding
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Indexed keywords
ASCORBIC ACIDS;
DIMETHYLDIDODECYLAMMONIUM BROMIDES;
DIRECT ELECTRON TRANSFER;
ELECTROCATALYTIC;
ELECTROCATALYTIC MECHANISM;
HEME GROUP;
HEME PROTEINS;
IN-SITU REACTIONS;
LIMITS OF DETECTION;
MODIFIED GLASSY CARBON ELECTRODE;
OPTIMAL CONDITIONS;
REDUCTION PEAK;
UNFOLDING;
BROMINE COMPOUNDS;
DENSITY FUNCTIONAL THEORY;
ELECTROCHEMISTRY;
GLASS MEMBRANE ELECTRODES;
HEMOGLOBIN;
ORGANIC ACIDS;
PORPHYRINS;
PROTEINS;
UREA;
NITRIC OXIDE;
ASCORBIC ACID;
DIDODECYLDIMETHYLAMMONIUM BROMIDE;
HEMOGLOBIN;
NITRIC OXIDE;
SODIUM NITRITE;
ACID;
CARBON;
HEME;
HEMOPROTEIN;
UREA;
ARTICLE;
CATALYSIS;
CHEMICAL INTERACTION;
CHEMICAL REACTION KINETICS;
CONCENTRATION (PARAMETERS);
CONTROLLED STUDY;
ELECTROCATALYSIS;
ELECTROCHEMICAL ANALYSIS;
ELECTRODE;
FIELD EMISSION SCANNING ELECTRON MICROSCOPY;
GLASSY CARBON ELECTRODE;
HEMOGLOBIN ANALYSIS;
LIMIT OF DETECTION;
MOLECULAR BIOLOGY;
MOLECULAR DYNAMICS;
PROTEIN DENATURATION;
PROTEIN UNFOLDING;
SPECTROPHOTOMETRY;
UNFOLDED PROTEIN RESPONSE;
CHEMICAL REACTION;
DEOXYGENATION;
ELECTRON TRANSPORT;
PROCESS DEVELOPMENT;
PROTEIN DEPLETION;
PROTEIN INTERACTION;
REDUCTION;
SENSITIVITY ANALYSIS;
BINDING SITE;
CHEMISTRY;
CONDUCTOMETRY;
EQUIPMENT;
EQUIPMENT DESIGN;
EQUIPMENT FAILURE;
GENETIC PROCEDURES;
PROTEIN ANALYSIS;
PROTEIN BINDING;
PROTEIN FOLDING;
REPRODUCIBILITY;
SENSITIVITY AND SPECIFICITY;
BINDING SITES;
BIOSENSING TECHNIQUES;
CATALYSIS;
CONDUCTOMETRY;
EQUIPMENT DESIGN;
EQUIPMENT FAILURE ANALYSIS;
HEMOGLOBINS;
NITRIC OXIDE;
PROTEIN BINDING;
PROTEIN FOLDING;
PROTEIN INTERACTION MAPPING;
REPRODUCIBILITY OF RESULTS;
SENSITIVITY AND SPECIFICITY;
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EID: 84870829694
PISSN: 09565663
EISSN: 18734235
Source Type: Journal
DOI: 10.1016/j.bios.2012.09.034 Document Type: Article |
Times cited : (23)
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References (34)
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