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Volumn 1382, Issue 1, 1998, Pages 129-136
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1H and 13C NMR studies of a truncated heme domain from Chlorella vulgaris nitrate reductase: Signal assignment of the heme moiety
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Author keywords
(Chlorella); 2D NMR; Cytochrome b; Heine protein; Nitrate reductace
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Indexed keywords
CYTOCHROME B5;
FLAVOPROTEIN;
HEME;
NITRATE REDUCTASE;
CARBON;
HYDROGEN;
PROTOPORPHYRIN;
ARTICLE;
CARBON NUCLEAR MAGNETIC RESONANCE;
CHLORELLA;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
ENZYME ANALYSIS;
ENZYME SUBUNIT;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE;
OXIDATION REDUCTION POTENTIAL;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTON NUCLEAR MAGNETIC RESONANCE;
ANIMAL;
BINDING SITE;
CATTLE;
CHEMICAL STRUCTURE;
CHEMISTRY;
ENZYMOLOGY;
LIVER;
METABOLISM;
METHODOLOGY;
OXIDATION REDUCTION REACTION;
PROTEIN CONFORMATION;
CHLORELLA VULGARIS;
ANIMALS;
BINDING SITES;
CARBON ISOTOPES;
CATTLE;
CHLORELLA;
CYTOCHROMES B5;
HEME;
HYDROGEN;
LIVER;
MODELS, MOLECULAR;
NITRATE REDUCTASE;
NITRATE REDUCTASES;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
OXIDATION-REDUCTION;
PROTEIN CONFORMATION;
PROTOPORPHYRINS;
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EID: 0032517897
PISSN: 01674838
EISSN: None
Source Type: Journal
DOI: 10.1016/S0167-4838(97)00160-X Document Type: Article |
Times cited : (7)
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References (38)
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