Active site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures

Biochemistry

Volumn 51, Issue 20, 2012, Pages 4147-4156

  Nagel, Zachary D ^a   Meadows, Corey W ^a   Dong, Ming ^b   Bahnson, Brian J ^b   Klinman, Judith P ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF DELAWARE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; CATALYSIS; CHAINS; ENZYMES; HYDROGEN; HYDROPHOBICITY;

ALCOHOL DEHYDROGENASE; CONFORMATIONAL SAMPLINGS; DONOR-ACCEPTOR DISTANCE; ELECTROSTATIC MODELING; HYDROPHOBIC ACTIVE SITES; KINETIC ISOTOPE EFFECTS; REDUCED TEMPERATURE DEPENDENCE; TEMPERATURE DEPENDENCE;

TEMPERATURE DISTRIBUTION;

ALCOHOL DEHYDROGENASE; ENZYME VARIANT; HYDROGEN; MUTANT PROTEIN; NICOTINAMIDE;

ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; HYDROGEN TUNNELING; HYDROPHOBICITY; MOLECULAR MODEL; MUTATION; PH; PKA; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT; STATIC ELECTRICITY; STEADY STATE; TEMPERATURE DEPENDENCE; WILD TYPE;

EID: 84861379052     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3001352     Document Type: Article

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