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Volumn 39, Issue 35, 2000, Pages 10884-10891
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FT-IR spectroscopic characterization of NADH:Ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain
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Author keywords
[No Author keywords available]
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Indexed keywords
BACTERIAL ENZYME;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);
ARTICLE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
FOURIER TRANSFORMATION;
INFRARED SPECTROSCOPY;
NONHUMAN;
OXIDATION;
PRIORITY JOURNAL;
PROTON TRANSPORT;
ALKANESULFONIC ACIDS;
ASPARTIC ACID;
BUFFERS;
ELECTROCHEMISTRY;
ELECTRON TRANSPORT COMPLEX I;
ESCHERICHIA COLI;
GLUTAMIC ACID;
IRON-SULFUR PROTEINS;
MODELS, CHEMICAL;
MORPHOLINES;
NADH, NADPH OXIDOREDUCTASES;
OXIDATION-REDUCTION;
PEPTIDE FRAGMENTS;
PROTON PUMPS;
SPECTROPHOTOMETRY, ULTRAVIOLET;
SPECTROSCOPY, FOURIER TRANSFORM INFRARED;
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EID: 0034609560
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi000842a Document Type: Article |
Times cited : (85)
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References (47)
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