Adjacent cysteines are capable of ligating the same tetranuclear iron-sulfur cluster

Proteins: Structure, Function and Genetics

Volumn 56, Issue 3, 2004, Pages 556-563

  Gurrath, Marion ^a   Friedrich, Thorsten ^b  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b UNIVERSITY OF FREIBURG   (Germany)

Author keywords

NiFe hydrogenase; Binding motif; Complex I; Metal coordination; Molecular modeling; NADH dehydrogenase

Indexed keywords

CYSTEINE; FLAVINE MONONUCLEOTIDE; IRON SULFUR PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

ARTICLE; BINDING SITE; COMPUTER MODEL; CONFORMATIONAL TRANSITION; ELECTRON TRANSPORT; ENERGY METABOLISM; MOLECULAR DYNAMICS; MUTAGENESIS; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON TRANSPORT; STEREOSPECIFICITY; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; BINDING SITES; COMPUTER SIMULATION; CYSTEINE; DESULFOVIBRIO GIGAS; DESULFOVIBRIO VULGARIS; ELECTRON TRANSPORT COMPLEX I; HYDROGENASE; LIGANDS; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 3142776181     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20155     Document Type: Article

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