The widespread occurrence of enzymatic hydrogen tunneling, and its unique properties, lead to a new physical model for the origins of enzyme catalysis

Procedia Chemistry

Volumn 3, Issue 1, 2011, Pages 291-305

  Klinman, Judith P ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Active site compression; Enzyme catalysis; Hydrogen tunneling; Kinetic isotope effects

Indexed keywords

CATALYSIS; CHEMICAL BONDS; DEUTERIUM; HYDROGEN; QUANTUM ELECTRONICS; VAN DER WAALS FORCES;

ACTIVE SITE; CONFORMATIONAL SAMPLINGS; DONOR-ACCEPTOR DISTANCE; ENZYME CATALYSIS; KINETIC ISOTOPE EFFECTS; NONADIABATIC MODELING; REACTION CONDITIONS; SITE-SPECIFIC MUTAGENESIS;

ENZYMES;

EID: 82655180690     PISSN: 18766196     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1016/j.proche.2011.08.037     Document Type: Conference Paper

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