How can a single second sphere amino acid substitution cause reduction midpoint potential changes of hundreds of millivolts?

Journal of the American Chemical Society

Volumn 129, Issue 32, 2007, Pages 9927-9940

  Yikilmaz, Emine ^a,b   Porta, Jason ^c   Grove, Laurie E ^d   Vahedi Faridi, Ardeschir ^c,e   Bronshteyn, Yuriy ^a   Brunold, Thomas C ^d   Borgstahl, Gloria E O ^c   Miller, Anne Frances ^a,b  

^a UNIVERSITY OF KENTUCKY   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

^c NEBRASKA MEDICAL CENTER   (United States)

^d UNIVERSITY OF WISCONSIN MADISON   (United States)

^e FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; HYDROGEN PEROXIDE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC SOLVENTS; PROTEINS; PROTONATION;

ISOELECTRONIC; ISOSTRUCTURAL; REDUCTION MIDPOINT; SUPEROXIDE DISMUTASE (SOD);

AMINO ACIDS;

FERROUS ION; GLUTAMINE; GLYCINE; HYDROGEN PEROXIDE; METAL; OXYGEN; SUPEROXIDE; SUPEROXIDE DISMUTASE; WATER;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; ENERGY TRANSFER; ENZYME ACTIVE SITE; HYDROGEN BOND; MOLECULAR STABILITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OPTICAL RESOLUTION; OXIDATION REDUCTION REACTION; PROTON TRANSPORT;

AMINO ACID SUBSTITUTION; BINDING SITES; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ELECTRON SPIN RESONANCE SPECTROSCOPY; FERRIC COMPOUNDS; FERROUS COMPOUNDS; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; HYDROGEN BONDING; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; SUPEROXIDE DISMUTASE;

EID: 34547884637     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja069224t     Document Type: Article

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