Atomic description of an enzyme reaction dominated by proton tunneling

Science

Volumn 312, Issue 5771, 2006, Pages 237-241

  Masgrau, Laura ^a,b,e   Roujeinikova, Anna ^a   Johannissen, Linus O ^a,b   Hothi, Parvinder ^a   Basran, Jaswir ^c   Ranaghan, Kara E ^d   Mulholland, Adrian J ^d   Sutcliffe, Michael J ^a,b   Scrutton, Nigel S ^a   Leys, David ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

^c UNIVERSITY OF LEICESTER   (United Kingdom)

^d UNIVERSITY OF BRISTOL   (United Kingdom)

^e INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AROMATIC COMPOUNDS; ELECTRON TUNNELING; ELEMENTARY PARTICLES; ENZYME KINETICS; MOLECULAR STRUCTURE; PROTONS; REACTION KINETICS;

ENZYME REACTION; ENZYME SYSTEM; ENZYME-CATALYZED REACTION; PROTON TUNNELING;

ENZYMES;

ARALKYLAMINE DEHYDROGENASE; AROMATIC AMINE; OXIDOREDUCTASE; OXYGEN; TRYPTAMINE; UNCLASSIFIED DRUG;

CATALYSIS; COMPUTER SIMULATION; ENZYME ACTIVITY; IMAGE RESOLUTION; OXIDATION; REACTION KINETICS;

ARTICLE; ATOMIC PARTICLE; CATALYSIS; CHEMICAL REACTION; COMPUTER SIMULATION; CRYSTAL STRUCTURE; ENZYME MECHANISM; OXIDATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; REACTION ANALYSIS; STRUCTURE ANALYSIS;

ALCALIGENES FAECALIS; ASPARTIC ACID; BINDING SITES; CATALYSIS; CHEMISTRY, PHYSICAL; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, CHEMICAL; MOTION; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; OXYGEN; PROTONS; TEMPERATURE; THERMODYNAMICS; TRYPTAMINES; WATER;

EID: 33645801770     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1126002     Document Type: Article

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51. This work was supported by the Lister Institute of Preventive Medicine (NSS), by the Biotechnology and Biological Sciences Research Council (BBSRC), and by the Engineering and Physical Sciences Research Council (EPSRC). A.J.M. thanks the IBM High Performance Computing Life Sciences Outreach Programme for support. M.J.S. gratefully acknowledges use of the University of Leicester Mathematical Modelling Centre's supercomputer, which was purchased through the EPSRC Strategic Equipment Initiative. D.L. is a Royal Society University Research Fellow and a European Molecular Biology Organisation (EMBO) Young Investigator. We gratefully acknowledge access to European Synchrotron Radiation Facility and to EMBL-Deutches Electronen Synchrotron beamlines with support from the European Community contract number RII3/CT/2004/5060008. Atomic coordinates and structure factor amplitudes have been deposited in the Protein Data Bank (PDB) (accession codes: 2AH1 for the free enzyme; 2AGL for the phenylhydrazine adduct; 2AGY and 2AGX for the Schiff-base intermediate in the form A and B crystals, respectively; 2AH0 and 2AGZ for the carbinolamine intermediate in the form A and C crystals, and 2AGW for the tryptamine-reduced AADH).