HHM motif at the CuH-Site of peptidylglycine monooxygenase is a pH-dependent conformational switch

Biochemistry

Volumn 52, Issue 15, 2013, Pages 2586-2596

  Kline, Chelsey D ^a   Mayfield, Mary ^a   Blackburn, Ninian J ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL SWITCHES; COORDINATING LIGANDS; FOURIER TRANSFORM INFRA REDS; MONOOXYGENASES; SECOND ELECTRONS; SPECTROSCOPIC PROPERTY; STRUCTURAL ELEMENTS; STRUCTURAL TRANSITIONS;

AMINO ACIDS; CATALYSIS; CATALYST ACTIVITY; ENZYMES; LIGANDS; MAGNETIC RESONANCE; NITROGEN; PARAMAGNETISM; PEPTIDES; X RAY ABSORPTION SPECTROSCOPY;

COPPER;

COPPER; HISTIDINE; OXYGEN; PEPTIDYLGLYCINE MONOOXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

ARTICLE; CATALYSIS; CHEMICAL INTERACTION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COVALENT BOND; ELECTRON; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; FOURIER TRANSFORM INFRARED PHOTOACOUSTIC SPECTROSCOPY; HYDROXYLATION; PH; PRIORITY JOURNAL; PROTON TRANSPORT; X RAY ABSORPTION SPECTROSCOPY;

AMINO ACID MOTIFS; CATALYTIC DOMAIN; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; OXYGEN; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84876217861     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4002248     Document Type: Article

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