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Journal of Biochemistry Advance Access published online on January 29, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm049
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© 2007 The Japanese Biochemical Society

Role of the conserved cysteine residues of the 11.5 kDa subunit in complex I catalytic properties

Isabel Marquesa,*, Alexandra V. Ushakovaa, Margarida Duartea and Arnaldo Videiraa,b

aIBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal
bICBAS - Instituto de Ciências Biomédicas de Abel Salazar, Universidade do Porto, Largo Prof. Abel Salazar 2, 4099-003 Porto, Portugal.

* Corresponding author: Fax: +351 226099157 E-mail address: imarques{at}ibmc.up.pt

Received November 29, 2006; Accepted January 23, 2007


  Abstract

Mitochondrial complex I exists as a mixture of two inter-convertible forms: active (A) and de-activated (D), the latter being sensitive to SH-modifying compounds. To investigate if the conserved cysteine-rich 11.5 kDa subunit of Neurospora crassa complex I is involved in this process, we subjected the corresponding genomic DNA to site-directed mutagenesis. The four cysteine residues of the subunit were separately substituted with serine residues and the resulting proteins were independently expressed in a null-mutant strain. All of the obtained mutant strains were able to assemble a complex I with similar kinetic properties to those observed in the wild-type enzyme, indicating that none of the cysteine residues of the 11.5 kDa protein is individually relevant for the A/D transition process. Diminished amounts of assembled complex I seem to be the major effect of these specific mutations.

Key Words: active/de-active transition, complex I, mitochondria, Neurospora crass, site-directed mutagenesis


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