Insights into flavin-based electron bifurcation via the nadh-dependent reduced ferredoxin:nadp oxidoreductase structure

Journal of Biological Chemistry

Volumn 290, Issue 36, 2015, Pages 21985-21995

  Demmer, Julius K ^a   Huang, Haiyan ^a   Wang, Shuning ^a   Demmer, Ulrike ^a   Thauer, Rudolf K ^a   Ermler, Ulrich ^a  

^a MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIFURCATION (MATHEMATICS); ENZYMES; METABOLISM;

CATALYTIC PROCESS; COMPLEX STRUCTURE; ENERGY METABOLISM; OXIDOREDUCTASES; PROSTHETIC GROUPS; REDOX CENTERS;

ELECTRONS;

ARGININE; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; BACTERIAL PROTEIN; FERREDOXIN; IRON SULFUR PROTEIN; MULTIPROTEIN COMPLEX; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN BINDING; RECOMBINANT PROTEIN; RIBOFLAVIN DERIVATIVE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CLUSTER ANALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; ELECTRON; ELECTRON TRANSPORT; ELECTRONBIFURCATION; ENERGY METABOLISM; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; MICROBIAL ENERGY METABOLISM; MOLECULAR DOCKING; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN BINDING; THERMOTOGA MARITIMA; X RAY; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR MODEL; OXIDATION REDUCTION REACTION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT; ELECTRONS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FERREDOXIN-NADP REDUCTASE; FERREDOXINS; FLAVINS; HYDROGEN BONDING; IRON-SULFUR PROTEINS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; NAD; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; THERMOTOGA MARITIMA;

EID: 84941312535     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.656520     Document Type: Article

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