The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: Quantum refinement

Biophysical Journal

Volumn 87, Issue 5, 2004, Pages 3437-3447

  Nilsson, Kristina ^a   Hersleth, Hans Petter ^b   Rod, Thomas H ^a   Andersson, K Kristoffer ^b   Ryde, Ulf ^a  

^a LUND UNIVERSITY   (Sweden)

^b UNIVERSITY OF OSLO   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

COMPOUND II; FERRIC ION; HYDROGEN PEROXIDE; METMYOGLOBIN; PEROXIDASE; UNCLASSIFIED DRUG; HISTIDINE; MYOGLOBIN; OXYGEN; PROTON;

ARTICLE; CRYSTALLOGRAPHY; ENERGY TRANSFER; HYDROGEN BOND; OXIDATION; PH; PROTON TRANSPORT; QUANTUM CHEMISTRY; THEORETICAL STUDY; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; COMPUTER SIMULATION; EVALUATION; OXIDATION REDUCTION REACTION; PROTEIN BINDING; PROTEIN CONFORMATION; QUANTUM THEORY;

BINDING SITES; COMPUTER SIMULATION; FERRIC COMPOUNDS; HISTIDINE; HYDROGEN PEROXIDE; MODELS, CHEMICAL; MODELS, MOLECULAR; MYOGLOBIN; OXIDATION-REDUCTION; OXYGEN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTONS; QUANTUM THEORY;

EID: 13844270250     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.041590     Document Type: Article

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