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Volumn 41, Issue 15, 2002, Pages 4827-4836
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The 1.25 Å resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement
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Author keywords
[No Author keywords available]
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Indexed keywords
CYTOCHROMES;
BACTERIOLOGY;
ELECTRON TRANSITIONS;
HYDROGEN BONDS;
NITROGEN OXIDES;
PROTEINS;
CYTOCHROME C;
HEME;
NITRATE;
NITRATE REDUCTASE;
NITRITE;
PROPIONIC ACID DERIVATIVE;
PROTEIN NAPB;
RECOMBINANT ENZYME;
UNCLASSIFIED DRUG;
PROTEIN SUBUNIT;
ARTICLE;
CRYSTAL STRUCTURE;
DESULFOVIBRIO;
ELECTRON TRANSPORT;
ENZYME ACTIVE SITE;
ENZYME MECHANISM;
ENZYME STRUCTURE;
ENZYME SUBUNIT;
HAEMOPHILUS INFLUENZAE;
HYDROGEN BOND;
OXIDATION REDUCTION POTENTIAL;
PRIORITY JOURNAL;
PROTEIN FOLDING;
REDUCTION;
BINDING SITE;
CHEMICAL STRUCTURE;
CHEMISTRY;
ENZYMOLOGY;
METABOLISM;
OXIDATION REDUCTION REACTION;
PROTEIN CONFORMATION;
X RAY CRYSTALLOGRAPHY;
BACTERIA (MICROORGANISMS);
DESULFOVIBRIO;
DESULFOVIBRIO DESULFURICANS;
HAEMOPHILUS;
HAEMOPHILUS INFLUENZAE;
BINDING SITES;
CATALYTIC DOMAIN;
CRYSTALLOGRAPHY, X-RAY;
CYTOCHROME C GROUP;
DESULFOVIBRIO;
HEME;
HYDROGEN BONDING;
MODELS, MOLECULAR;
NITRATE REDUCTASE;
NITRATE REDUCTASES;
OXIDATION-REDUCTION;
PROPIONATES;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN SUBUNITS;
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EID: 0037117405
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi012144b Document Type: Article |
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Times cited : (44)
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References (53)
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