Redox properties of the prosthetic groups of Na+-translocating NADH:Quinone oxidoreductase. 2. Study of the enzyme by optical spectroscopy

Biochemistry

Volumn 48, Issue 27, 2009, Pages 6299-6304

  Bogachev, Alexander V ^a   Bloch, Dmitry A ^b   Bertsova, Yulia V ^a   Verkhovsky, Michael I ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

ANION RADICALS; COFACTORS; CONCENTRATION OF; ELECTRON-TRANSFER STEP; ELECTRONIC SPECTRUM; ONE-ELECTRON REDUCTIONS; OPTICAL SPECTROSCOPY; OXIDO-REDUCTION; OXIDOREDUCTASE; PH DEPENDENCE; PH VALUE; PROSTHETIC GROUPS; PROTON UPTAKE; REDOX POTENTIALS; REDOX PROPERTY; REDOX TITRATIONS; REDOX TRANSITION; SEMIQUINONE; SODIUM IONS; TWO-ELECTRON REDUCTION;

ELECTRONS; FREE RADICAL REACTIONS; METAL IONS; NEGATIVE IONS; PROSTHETICS;

ENZYMES;

IRON SULFUR PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (QUINONE); RIBOFLAVIN; SEMIQUINONE; SODIUM ION;

ARTICLE; ELECTROCHEMISTRY; ELECTRON TRANSPORT; ENZYME ANALYSIS; MOLECULAR MODEL; NONHUMAN; OPTICAL SPECTROSCOPY; OXIDATION REDUCTION REACTION; PH; PRIORITY JOURNAL; PROTON TRANSPORT; SPECTROSCOPY; TITRIMETRY; VIBRIO HARVEYI;

ELECTROCHEMISTRY; HYDROGEN-ION CONCENTRATION; ION TRANSPORT; QUINONE REDUCTASES; QUINONES; RIBOFLAVIN; SODIUM; SPECTRUM ANALYSIS;

VIBRIO HARVEYI;

EID: 67650080517     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900525v     Document Type: Article

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