Analysis of compound heterozygous and homozygous mutations found in peripheral subunits of human respiratory Complex I, NDUFS1, NDUFS2, NDUFS8 and NDUFV1, by modeling in the E. coli enzyme.
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Subunits E-F-G of E. coli Complex I can form an active complex when expressed alone, but in time-delayed assembly co-expression of B-CD-E-F-G is optimal.
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Human clinical mutations in mitochondrially encoded subunits of Complex I can be successfully modeled in E. coli.
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Analysis of the assembly pathway for membrane subunits of Complex I reveals that subunit L (ND5) can assemble last in E. coli.
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The transmembrane helices of the L, M, and N subunits of Complex I from E. coli can be assigned on the basis of conservation and hydrophobic moment analysis.
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A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.
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Chemical modification of mono-cysteine mutants allows a more global look at conformations of the epsilon subunit of the ATP synthase from Escherichia coli.
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A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase.
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Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1Fo ATP synthase.
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The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli.
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Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone.
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