Titration of E. coli transhydrogenase domain III with bound NADP + or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1707, Issue 2-3, 2005, Pages 254-258

  Pedersen, Anders ^a   Johansson, Tomas ^b   Rydström, Jan ^a   Goran Karlsson B ^a,b  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

^b CHALMERS UNIVERSITY OF TECHNOLOGY   (Sweden)

Author keywords

Conformational change; Domain III; NADP(H); NMR; pH titration; Proton translocating transhydrogenase

Indexed keywords

AMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; MICHAELIS CONSTANT; NUCLEAR MAGNETIC RESONANCE; OXIDATION REDUCTION REACTION; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; RHODOSPIRILLUM RUBRUM; STRUCTURE ANALYSIS; TITRIMETRY;

ESCHERICHIA COLI; RHODOSPIRILLUM RUBRUM;

EID: 18044382697     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.12.004     Document Type: Article

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