A Structural Perspective on Respiratory Complex I: Structure by Rouslan G. Efremov, Leonid Sazanov (auth.), Leonid Sazanov

A Structural Perspective on Respiratory Complex I: Structure by Rouslan G. Efremov, Leonid Sazanov (auth.), Leonid Sazanov

By Rouslan G. Efremov, Leonid Sazanov (auth.), Leonid Sazanov (eds.)

The booklet includes chapters written by way of leaders within the study at the constitution and serve as of breathing complicated I. it is going to supply a concise and authoritative precis of the present wisdom on complicated I of respiration chains. This enzyme is valuable to strength metabolism and is implicated in lots of human neurodegenerative ailments, in addition to in getting older. till lately it used to be poorly understood on a structural point, and this publication will offer a well timed reference source. this type of booklet was once no longer released formerly. The final time a minireview sequence on advanced I have been released used to be in 2001, and because then complicated I box replaced particularly dramatically.

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Additional resources for A Structural Perspective on Respiratory Complex I: Structure and Function of NADH:ubiquinone oxidoreductase

Example text

Noteworthy, within this model water molecules at the interface between the subunits play an essential role as mediators for electron transfer accelerating the electron transfer reaction rate. To determine whether these water molecules exist, a structure of the peripheral arm of the complex at a much higher resolution is definitively needed. 2 Role of Cluster N1a The binuclear Fe/S cluster N1a is not part of the electron transfer chain from the FMN to the putative (ubi)quinone binding site. Its binding motif is present in the sequence of all homologues of NuoE.

It is bound to the C-terminal domain of NuoG in a few bacteria such as E. coli, A. aeolicus and T. thermophilus. 5 Å, thus, it seems more than unlikely that N7 participates in the electron transfer reaction to (ubi)quinone (Sazanov and Hinchliffe 2006). It seems to represent an evolutionary relic of a complex I ancestor with a different enzymatic function. Phylogenetic analysis revealed the presence of a common complex I progenitor present in the three domains of life containing the ‘minimal’ subunits with the exception of NuoE, F, and G (Friedrich et al.

2010) suggests that this arm is involved in proton translocation most 2 On the Mechanism of the Respiratory Complex I 25 Fig. 1 Scheme of (a) the E. coli nuo-operon and (b) of complex I. (a) shows the name and the sequence of the nuo genes on the E. coli chromosome. Genes coding for globular proteins constituting the peripheral arm are shown in white, genes coding for polytopic proteins constituting the membrane arm are shown in grey. (b) represents a model of complex I with the peripheral arm shown in white and the membrane arm in grey.

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