Two Distinct Regions of the Yeast Mitochondrial ADP/ATP Carrier Are Photolabeled by a New ADP Analogue:  2-Azido-3‘-O-naphthoyl-[β-32P]ADP. Identification of the Binding Segments by Mass Spectrometry

Author:

Dianoux Anne-Christine1,Noël Florence1,Fiore Christelle1,Trézéguet Véronique1,Kieffer Sylvie1,Jaquinod Michel1,Guy J.-M. Lauquin, and 1,Brandolin Gérard1

Affiliation:

1. Laboratoire de Biophysique et Biochimie des Systèmes Intégrés, CNRS−UMR 5092, DBMS, CEA-Grenoble, 17 Rue des Martyrs, 38054 Grenoble Cedex 9, France, Laboratoire de Physiologie Moléculaire et Cellulaire, IBGC−CNRS, 1 Rue Camille Saint-Saëns, 33077 Bordeaux Cedex, France, Laboratoire de Chimie des Protéines, DBMS, CEA-Grenoble, 17 Rue des Martyrs, 38054 Grenoble Cedex 9, France, and Laboratoire de Spectrométrie de Masse des Protéines, IBS, 41 rue Jules Horowitz, 38027 Grenoble, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

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1. Substrate binding in the mitochondrial ADP/ATP carrier is a step-wise process guiding the structural changes in the transport cycle;Nature Communications;2022-06-23

2. Utilities of Anti-ligand Antibody and Mass Spectrum to Elucidate Photolabeled Sites;Photoaffinity Labeling for Structural Probing Within Protein;2017

3. The substrate specificity of the human ADP/ATP carrier AAC1;Molecular Membrane Biology;2012-11-23

4. Yeast ADP/ATP Carrier Isoform 2;Journal of Biological Chemistry;2011-10

5. Coenzyme A enhances activity of the mitochondrial adenine nucleotide translocator;The International Journal of Biochemistry & Cell Biology;2010-01

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