EPR Spectroscopy of VO2+-ATP Bound to Catalytic Site 3 of Chloroplast F1-ATPase from ChlamydomonasReveals Changes in Metal Ligation Resulting from Mutations to the Phosphate-binding Loop Threonine (βT168)-Reference-Cited by-同舟云学术

EPR Spectroscopy of VO2+-ATP Bound to Catalytic Site 3 of Chloroplast F1-ATPase from ChlamydomonasReveals Changes in Metal Ligation Resulting from Mutations to the Phosphate-binding Loop Threonine (βT168)

Published:1999-03 Issue:11 Volume:274 Page:7089-7094
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Chen Wei,LoBrutto Russell,Frasch Wayne D.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference40 articles.

1. Catalytic mechanism of F1-ATPase

2. Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase.

3. Mechanism of phosphorylation catalyzed by chloroplast coupling factor 1. Stereochemistry

4. Characterization of Ligands of a High-Affinity Metal-Binding Site in the Latent Chloroplast F1-ATPase by EPR Spectroscopy of Bound VO2+

5. Specific Tryptophan Substitution in Catalytic Sites of Escherichia coli F1-ATPase Allows Differentiation between Bound Substrate ATP and Product ADP in Steady-state Catalysis

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