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Volumn 405, Issue 1, 2002, Pages 87-94
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Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2
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Author keywords
Cupric reductase; Cuprous copper; Heavy metal associated domain; NADH dehydrogenase luminescence; Secondary structure prediction; Topology model
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Indexed keywords
BACTERIAL ENZYME;
COPPER;
EDETIC ACID;
FLAVOPROTEIN;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE 2;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
ARTICLE;
ATOMIC ABSORPTION SPECTROMETRY;
BINDING SITE;
BIOINFORMATICS;
CARBOXY TERMINAL SEQUENCE;
CHELATION;
CHROMATOPHORE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME BINDING;
ENZYME CONFORMATION;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
LUMINESCENCE;
NONHUMAN;
OXIDATION REDUCTION STATE;
OXIDATIVE STRESS;
PREDICTION;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN SECONDARY STRUCTURE;
RESPIRATORY CHAIN;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
BINDING SITES;
COPPER;
CYTOPLASM;
ELECTRON TRANSPORT;
ESCHERICHIA COLI;
MODELS, GENETIC;
MOLECULAR SEQUENCE DATA;
NADH DEHYDROGENASE;
ORGANOMETALLIC COMPOUNDS;
OXIDATIVE STRESS;
PHYLOGENY;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
SPECTROPHOTOMETRY;
TIME FACTORS;
ESCHERICHIA COLI;
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EID: 0036718981
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/S0003-9861(02)00277-1 Document Type: Article |
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Times cited : (47)
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References (34)
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