A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release

European Journal of Biochemistry

Volumn 268, Issue 5, 2001, Pages 1430-1438

  Rodrigues, Daniel J ^a   Venning, Jamie D ^a   Quirk, Philip G ^a   Baz Jackson, J ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

Ion pumps; Nucleotide binding; Proton translocation; Rhodosprillum rubrum; Transhydrogenase

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; CONTROLLED STUDY; IONIZATION; NONHUMAN; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTON TRANSPORT; RHODOSPIRILLUM RUBRUM; SITE DIRECTED MUTAGENESIS; STEADY STATE;

AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; FLUORESCENCE; HYDROGEN; HYDROGEN-ION CONCENTRATION; KINETICS; MUTATION; NADP; NADP TRANSHYDROGENASE; NUCLEOTIDES; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PROTONS; RHODOSPIRILLUM RUBRUM; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

RHODOSPIRILLUM RUBRUM;

EID: 0035086791     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02008.x     Document Type: Article

References (38)

1. Altered amino-acid metabolism in LRP mutants of Escherichia coli K12 and their derivatives
2. Proton translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to the fine regulation of the tricarboxylic acid cycle activity in mitochondria
3. The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labelling
4. Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex
5. Structure and Mechanism of proton-translocating transhydrogenase
6. The high resolution structure of the NADP (H) -binding component of proton-translocating transhydrogenase from human-heart mitochondria
7. Crystal structure of transhydrogenase domain III at 1.2 A resolution
8. Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum
9. Evidence that the transfer of hydride equivalents between nucleotides by proton-translocating transhydrogenase is direct
10. Properties of the soluble polypeptide of the proton-translocating transhydrogenase from Rhodospirillum rubrum obtained by expression in Escherichia coli
11. Interaction of nucleotides with the NAD (H) -binding domain of the proton-translocating transhydrogenase of Rhodospirillum rubrum
12. The binding of nucleotides to domain I proteins of the proton-translocating transhydrogenases of Rhodospirillum rubrum and Escherichia coli as measured by equilibrium dialysis
13. Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum
14. Proton-translocating transhydrogenase. Reconstitution of the extramembranous nucleotide-binding domains
15. High cyclic transhydrogenase activity catalysed by expressed an reconstituted nucleotide-binding domains of Rhodospirillum rubrum transhydrogenase
16. Structural and catalytic properties of the expressed and purified NAD(H)- and NADP(H)-binding domains of proton-pumping transhydrogenase from Escherichia coli
17. Catalytic properties of hybrid complexes of the NAD(H)-binding and NADP(H)-binding domains of the proton-translocating transhydrogenases from Escherichia coli and Rhodospirillum rubrum
18. A catalytically active complex formed from the recombinant dI protein of Rhodospirillum rubrum transhydrogenase, and the recombinant dIII protein of the human enzyme
19. Stopped-flow kinetics of hydride transfer between nucleotides by recombinant domains of proton-translocating transhydrogenase
20. A shift in the equilibrium constant at the catalytic site of proton-translocating transhydro-genase: Significance for a 'binding-change' mechanism
21. Stopped-flow reaction kinetics of recombinant components of proton-translocating transhydrogenase with physiological nucleotides
22. Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with nucleotide substrate analogues
23. Nicotinamide nucleotide transhydrogenase: A model for utilization of substrate binding energy for proton translocation
24. Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties
25. Interdomain hydride transfer in proton-translocating transhydrogenase
26. Sequence-specific resonance assignments for the NADP (H) -binding component (domain III) of proton-translocating transhydrogenase from Rhodospirillum rubrum
27. + in the dIII components of proton-translocating transhydrogenase from Homo sapiens and from Rhodospirillum rubrum by measurement of tryptophan fluorescence
28. New methods for quantitative determination of serum proteins separated by paper chromatography
29. Structural changes in the recombinant, NADP(H)-binding component (dIII) of proton-translocating transhydrogenase revealed by NMR spectroscopy
30. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
31. The pH dependences of reactions catalysed by the complete proton-translocating transhydrogenase from Rhodosprillum rubrum, and by the complex formed from its recombinant peripheral, nucleotide-binding domains
32. Mutations at Tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer
33. Towards understanding tryptophan fluorescence in proteins
34. Identification of an aspartic acid residue in the beta subunit which is essential for catalysis and proton pumping by transhydrogenase from Escherichia coli
35. Mapping of residues in the NADP (H) -binding site of proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli: A study of structure and function
36. NMR characterisation of the NADP (H) -binding domain of Escherichia coli transhydrogenase: Sequential assignment and global fold
37. The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli
38. Mutation of conserved residues in the NADP (H) -binding domain of the proton-translocating transhydrogenase of Escherichia coli