Conformation-specific crosslinking of mitochondrial complex I

Margherita Ciano, Matthew Fuszard, Heinrich Heide, Catherine H. Botting, Alexander Galkin

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)


Complex I is the only component of the eukaryotic respiratory chain of which no high-resolution structure is yet available. A notable feature of mitochondrial complex I is the so-called active/de-active conformational transition of the idle enzyme from the active (A) to the de-active, (D) form. Using an amine- and sulfhydryl-reactive crosslinker of 6.8 Å length (SPDP) we found that in the D-form of complex I the ND3 subunit crosslinked to the 39 kDa (NDUFA9) subunit. These proteins could not be crosslinked in the A-form. Most likely, both subunits are closely located in the critical junction region connecting the peripheral hydrophilic domain to the membrane arm of the enzyme where the entrance path for substrate ubiquinone is and where energy transduction takes place.
Original languageEnglish
Pages (from-to)867-872
Number of pages6
JournalFEBS Letters
Early online date27 Feb 2013
Publication statusPublished - 02 Apr 2013


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