PMID- 23438074
OWN - NLM
STAT- MEDLINE
DCOM- 20130613
LR  - 20130722
IS  - 1742-4658 (Electronic)
IS  - 1742-464X (Linking)
VI  - 280
IP  - 8
DP  - 2013 Apr
TI  - Communication between (L)-galactono-1,4-lactone dehydrogenase and cytochrome c.
PG  - 1830-40
LID - 10.1111/febs.12207 [doi]
AB  - l-galactono-1,4-lactone dehydrogenase (GALDH) catalyzes the terminal step of 
      vitamin C biosynthesis in plant mitochondria. Here we investigated the 
      communication between Arabidopsis thaliana GALDH and its natural electron 
      acceptor cytochrome c (Cc). Using laser-generated radicals we observed the 
      formation and stabilization of the GALDH semiquinone anionic species (GALDHSQ ). 
      GALDHSQ oxidation by Cc exhibited a nonlinear dependence on Cc concentration 
      consistent with a kinetic mechanism involving protein-partner association to form 
      a transient bimolecular complex prior to the electron transfer step. Oxidation of 
      GALDHSQ by Cc was significantly impaired at high ionic strength, revealing the 
      existence of attractive charge-charge interactions between the two reactants. 
      Isothermal titration calorimetry showed that GALDH weakly interacts with both 
      oxidized and reduced Cc. Chemical shift perturbations for (1) H and (15) N nuclei 
      of Cc, arising from the interactions with unlabeled GALDH, were used to map the 
      interacting surface of Cc. For Arabidopsis Cc and yeast Cc, similar residues are 
      involved in the interaction with GALDH. These residues are confined to a single 
      surface surrounding the heme edge. The range of chemical shift perturbations for 
      the physiological Arabidopsis Cc-GALDH complex is larger than that of the 
      non-physiological yeast Cc-GALDH complex, indicating that the former complex is 
      more specific. In summary, the results point to a relatively low affinity 
      GALDH-Cc interaction, similar for all partner redox states, involving 
      protein-protein dynamic motions. Evidence is also provided that Cc utilizes a 
      conserved surface surrounding the heme edge for the interaction with GALDH and 
      other redox partners. DATABASE: NMR assignment of the backbone amide resonances 
      of Arabidopsis CcRED has been deposited in BMRB database (BMRB accession number 
      18828). L-galactono-1,4-lactone dehydrogenase (L-galactono-1,4-lactone: 
      ferricytochrome c oxidoreductase, EC 1.3.2.3).
CI  - (c) 2013 The Authors Journal compilation (c) 2013 FEBS.
FAU - Hervas, Manuel
AU  - Hervas M
AD  - Instituto de Bioquimica Vegetal y Fotosintesis, CSIC and University of Sevilla, 
      Spain.
FAU - Bashir, Qamar
AU  - Bashir Q
FAU - Leferink, Nicole G H
AU  - Leferink NG
FAU - Ferreira, Patricia
AU  - Ferreira P
FAU - Moreno-Beltran, Blas
AU  - Moreno-Beltran B
FAU - Westphal, Adrie H
AU  - Westphal AH
FAU - Diaz-Moreno, Irene
AU  - Diaz-Moreno I
FAU - Medina, Milagros
AU  - Medina M
FAU - de la Rosa, Miguel A
AU  - de la Rosa MA
FAU - Ubbink, Marcellus
AU  - Ubbink M
FAU - Navarro, Jose A
AU  - Navarro JA
FAU - van Berkel, Willem J H
AU  - van Berkel WJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130325
PL  - England
TA  - FEBS J
JT  - The FEBS journal
JID - 101229646
RN  - 9007-43-6 (Cytochromes c)
RN  - EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors)
RN  - EC 1.3.2.3 (galactonolactone dehydrogenase)
SB  - IM
MH  - Calorimetry
MH  - Cytochromes c/*chemistry
MH  - Magnetic Resonance Spectroscopy
MH  - Oxidation-Reduction
MH  - Oxidoreductases Acting on CH-CH Group Donors/*chemistry
EDAT- 2013/02/27 06:00
MHDA- 2013/06/14 06:00
CRDT- 2013/02/27 06:00
PHST- 2012/12/04 00:00 [received]
PHST- 2013/02/08 00:00 [revised]
PHST- 2013/02/19 00:00 [accepted]
PHST- 2013/02/27 06:00 [entrez]
PHST- 2013/02/27 06:00 [pubmed]
PHST- 2013/06/14 06:00 [medline]
AID - 10.1111/febs.12207 [doi]
PST - ppublish
SO  - FEBS J. 2013 Apr;280(8):1830-40. doi: 10.1111/febs.12207. Epub 2013 Mar 25.