Conformation‐specific crosslinking of mitochondrial complex I. Issue 7 (27th February 2013)

• Record Type: Journal Article
• Authors: Ciano, Margherita; Fuszard, Matthew; Heide, Heinrich; Botting, Catherine H.; Galkin, Alexander
• Is Part Of: FEBS letters. Volume 587:Issue 7(2013)
• Page Start: 867
• Page End: 872
• Publication Date: 2013-02-27
• Subjects: DTNB -- 5, 5′-dithiobis-(2-nitrobenzoic acid) -- DTT -- dithiothreitol -- HAR -- hexaammineruthenium(III)-chloride -- NEM -- N-ethylmaleimide -- nLC-ESI-MSMS -- nano-HPLC electrospray ionization multistage tandem mass spectrometry -- ROS -- reactive oxygen species -- SMP -- submitochondrial particles -- SPDP -- N-succinimidyl 3-(2-pyridyldithio) propionate -- Mitochondrial complex I -- A/D transition -- ND3 subunit -- 39 kDa subunit -- NDUFA9 -- SPDP -- Crosslinking; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.02.039
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : ND3 and NDUFA9 physically interact by cross‐linking study (View interaction) Abstract : ► Active and dormant forms of mitochondrial complex I were assessed by crosslinking. ► ND3 and 39 kDa subunits were specifically crosslinked only in the dormant form. ►No conformation‐specific crosslinking were found in the active form. ► In mitochondria complex I 39 kDa subunit is located close to ND3.