Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain

Journal of Biological Chemistry

Volumn 281, Issue 16, 2006, Pages 11357-11365

  Maklashina, Elena ^a,b   Iverson, Tina M ^c,f   Sher, Yelizaveta ^a,g   Kotlyar, Violetta ^a   André, Juni ^c   Mirza, Osman ^c,h   Hudson, Janette M ^d   Armstrong, Fraser A ^d   Rothery, Richard A ^e   Weiner, Joel H ^e   Cecchini, Gary ^a,b  

^a SAN FRANCISCO VETERANS AFFAIRS MEDICAL CENTER   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

^e UNIVERSITY OF ALBERTA   (Canada)

^f VANDERBILT UNIVERSITY   (United States)

^g WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^h UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; ENZYMES; MUTAGENESIS; SUBSTITUTION REACTIONS;

FLAVIN BINDING DOMAIN; FUMARATE REDUCTASE; MUTANT ENZYMES; SUCCINATE:UBIQUINONE OXIDOREDUCTASE;

ESCHERICHIA COLI;

ALANINE; FUMARATE REDUCTASE; GLUTAMIC ACID; GLUTAMINE; QUERCETIN; SUCCINATE DEHYDROGENASE;

AMINO ACID SUBSTITUTION; AMINO ACID SYNTHESIS; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ESCHERICHIA COLI; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE BINDING SITE; PH; POTENTIOMETRY; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

ALANINE; AMINO ACIDS; BINDING SITES; CATALYSIS; ELECTROCHEMISTRY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX IV; ELECTRONS; ENZYME ACTIVATION; ESCHERICHIA COLI; FLAVINS; FUMARATES; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXIDOREDUCTASES; OXYGEN; PLASMIDS; POTENTIOMETRY; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SUCCINATE DEHYDROGENASE; SYNCHROTRONS; X-RAY DIFFRACTION;

ESCHERICHIA COLI;

EID: 33744960410     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M512544200     Document Type: Article

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