Modifications of protein environment of the [2Fe-2S] cluster of the bc 1 complex: Effects on the biophysical properties of the Rieske iron-sulfur protein and on the kinetics of the complex

Journal of Biological Chemistry

Volumn 285, Issue 12, 2010, Pages 9233-9248

  Lhee, Sangmoon ^a   Kolling, Derrick R J ^a   Nair, Satish K ^a   Dikanov, Sergei A ^a   Crofts, Antony R ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL PROPERTIES; CONCENTRATION OF; DRIVING FORCES; ELECTROCHEMICAL CHARACTERISTICS; ELECTRON MODELS; ELECTRON SPIN-ECHO ENVELOPE MODULATIONS; ELECTRON TRANSFER; H-BONDING; H-BONDS; HIGH POTENTIAL; IRON-SULFUR PROTEINS; OVERALL REACTIONS; PROTEIN FILM VOLTAMMETRY; RATE DETERMINING STEP; RHODOBACTER SPHAEROIDES; SITE-DIRECTED MUTATION; SULFUR ATOMS; UBIQUINOL;

AMINO ACIDS; ELECTRON AFFINITY; ELECTRONS; INTERNET SERVICE PROVIDERS; PHOSPHATASES; PROTEINS; PROTONS; REACTION RATES; SPIN DYNAMICS; SULFUR;

IRON COMPOUNDS;

IRON SULFUR PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE; ANTIMYCIN A1; DRUG DERIVATIVE; UBIQUINOL; UBIQUINONE;

ACTION POTENTIAL; ARTICLE; CONTROLLED STUDY; ELECTROCHEMISTRY; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME SUBSTRATE COMPLEX; GENE CLUSTER; HYDROGEN BOND; LIGAND BINDING; MUTATIONAL ANALYSIS; NONHUMAN; POTENTIOMETRY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; RHODOBACTER SPHAEROIDES; STRUCTURE ANALYSIS; THERMODYNAMICS; BIOPHYSICS; CHEMICAL MODEL; CHEMISTRY; CIRCULAR DICHROISM; METABOLISM; METHODOLOGY; MUTATION; PH; SITE DIRECTED MUTAGENESIS;

RHODOBACTER SPHAEROIDES;

ANTIMYCIN A; BIOPHYSICS; CIRCULAR DICHROISM; ELECTROCHEMISTRY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX III; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; IRON-SULFUR PROTEINS; MODELS, CHEMICAL; MUTAGENESIS, SITE-DIRECTED; MUTATION; RHODOBACTER SPHAEROIDES; UBIQUINONE;

EID: 77950567917     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.043505     Document Type: Article

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