Pinpoint chemical modification of Asp160 in the 49 kDa subunit of bovine mitochondrial complex I via a combination of ligand-directed Tosyl chemistry and click chemistry

Biochemistry

Volumn 53, Issue 49, 2014, Pages 7816-7823

  Masuya, Takahiro ^a   Murai, Masatoshi ^a   Morisaka, Hironobu ^a   Miyoshi, Hideto ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ANALYSIS; CHEMICAL MODIFICATION; LIGANDS; MAMMALS; MITOCHONDRIA; SYNTHESIS (CHEMICAL);

CHEMICAL EQUATIONS; MITOCHONDRIAL COMPLEX; PROTEOMIC ANALYSIS; REACTION PARTNERS; REACTION YIELDS; STRUCTURAL FEATURE; SUBMITOCHONDRIAL PARTICLES; TERMINAL ALKYNE;

IODINE;

ACETOGENIN; ALKYNE; ASPARTIC ACID; BULLATACIN; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RHODAMINE; UBIQUINONE; BENZOIC ACID DERIVATIVE; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; ENZYME INHIBITOR; FENPYROXIMATE; FURAN DERIVATIVE; LIGAND; PROTEIN SUBUNIT; PYRAZOLE DERIVATIVE; QUINAZOLINE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; TOLUENESULFONIC ACID DERIVATIVE;

ALKYNYLATION; ANIMAL TISSUE; ARTICLE; CATTLE; CLICK CHEMISTRY; CONTROLLED STUDY; ENZYME MODIFICATION; ENZYME SPECIFICITY; HEART; LIGAND DIRECTED TOSYL CHEMISTRY; NONHUMAN; PROTEOMICS; SUBMITOCHONDRIAL PARTICLE; SYNTHESIS; ANIMAL; ANTAGONISTS AND INHIBITORS; BOVINAE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DRUG EFFECTS; ENZYME ACTIVE SITE; ENZYMOLOGY; HEART MITOCHONDRION; METABOLISM; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN SUBUNIT;

BOVINAE;

ACETOGENINS; ANIMALS; ASPARTIC ACID; BENZOATES; CATALYTIC DOMAIN; CATTLE; CLICK CHEMISTRY; ELECTRON TRANSPORT COMPLEX I; ENZYME INHIBITORS; FURANS; INDICATORS AND REAGENTS; LIGANDS; MITOCHONDRIA, HEART; MODELS, MOLECULAR; MOLECULAR WEIGHT; NADH DEHYDROGENASE; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PYRAZOLES; QUINAZOLINES; TOSYL COMPOUNDS;

EID: 84918561145     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501342w     Document Type: Article

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