Addition/Correction pubs.acs.org/biochemistry
Correction to Mitochondrial ADP/ATP Carrier: Preventing Conformational Changes by Point Mutations Inactivates Nucleotide Transport Activity Marion Babot, Corinne Blancard, Igor Zeman, Guy J.-M. Lauquin, and Véronique Trézéguet* Biochemistry 2012, 51 (37), 7348−7356. DOI: 10.1021/bi300978z
T
he Kd value for ATR binding should be in nanomolar instead of micromolar. The corrected table is below:
Table 2. Kinetic Parameters of the ScAnc2p Variants ADP/ATP exchange parametersa WT ScAnc2p ScAnc2pCys73Trp ScAnc2pTyr97Cys‑Gly298Ser
N-ADP bindingb
ATR bindingc
VmaxADP (nmol min−1 mg−1)
KMADP (μM)
K1/2 (μM)
BmaxATR (pmol/mg)
KdATR (nM)
87 ± 5 10 ± 1 12 ± 1
1.5 ± 0.2 3.4 ± 0.8 0.31 ± 0.09
1.1 ± 0.2 3.4 ± 1.2 6.2 ± 2.1
1010 ± 77 NMd 344 ± 11
192 ± 25 NMd 89 ± 11
a
The ADP/ATP exchange was followed at 340 nm with freshly isolated mitochondria. The given values are the means of three to six different experiments. bVarious concentrations of N-ADP were added to isolated mitochondria (0.5 mg/mL). cVarious [3H]ATR concentrations were incubated with isolated mitochondria (1 mg). BMaxATR is the maximal number of ATR binding sites. dNonmeasurable.
Published: April 15, 2016 © 2016 American Chemical Society
2422
DOI: 10.1021/acs.biochem.6b00310 Biochemistry 2016, 55, 2422−2422
