The NADH oxidation domain of Complex I: Do bacterial and mitochondrial enzymes catalyze ferricyanide reduction similarly?

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1459, Issue 1, 2000, Pages 61-68

  Zickermann, Volker ^a   Kurki, Sari ^a   Kervinen, Marko ^b   Hassinen, Ilmo ^b   Finel, Moshe ^a  

^a BIOMEDICUM HELSINKI   (Finland)

^b UNIVERSITY OF OULU   (Finland)

Author keywords

Deamino NADH; Fe S cluster; FMN; NADH; NDH 1; Ubiquinone

Indexed keywords

CYTOCHROME B5 REDUCTASE; DICYCLOHEXYLCARBODIIMIDE; FERRICYANIDE; MITOCHONDRIAL ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; CATALYSIS; CATTLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; NONHUMAN; PARACOCCUS DENITRIFICANS; PRIORITY JOURNAL; REDUCTION;

ANIMALS; BACTERIA; BINDING SITES; CATTLE; DICYCLOHEXYLCARBODIIMIDE; ELECTRON TRANSPORT COMPLEX I; FERRICYANIDES; HYDROGEN-ION CONCENTRATION; KINETICS; MITOCHONDRIA, HEART; NAD; NADH, NADPH OXIDOREDUCTASES; OXIDATION-REDUCTION; PARACOCCUS DENITRIFICANS; ROTENONE; RUTHENIUM COMPOUNDS;

BACTERIA (MICROORGANISMS); BOVINAE; PARACOCCUS DENITRIFICANS;

EID: 0034691754     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(00)00113-4     Document Type: Article

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