By Rouslan G. Efremov, Leonid Sazanov (auth.), Leonid Sazanov (eds.)
The e-book includes chapters written via leaders within the study at the constitution and serve as of breathing complicated I. it's going to offer a concise and authoritative precis of the present wisdom on advanced I of respiration chains. This enzyme is important to strength metabolism and is implicated in lots of human neurodegenerative illnesses, in addition to in getting older. until eventually lately it was once poorly understood on a structural point, and this e-book will offer a well timed reference source. the sort of ebook used to be now not released formerly. The final time a minireview sequence on advanced I have been released used to be in 2001, and because then advanced I box replaced relatively dramatically.
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Additional info for A Structural Perspective on Respiratory Complex I: Structure and Function of NADH:ubiquinone oxidoreductase
The substrate (ubi)quinone is most likely directly reduced by one of the Fe/S clusters. The exact location of the (ubi)quinone-binding site is not yet known, but based on (ubi)quinone-site inhibitor studies and inhibitor resistance of site-directed mutants it is expected to be located at the interface between the peripheral and the membrane arm (Darrouzet et al. 1998; Schuler et al. 1999; Murai et al. 2009; Tocilescu et al. 2010). The membrane arm does not contain a conserved motif for binding any further cofactors.
Friedrich et al. that such a cluster connecting N7 with the electron pathway to (ubi)quinone reduction site is indeed present in NuoG (Peng et al. 2010). The late acquisition of NuoG and the separate and subsequent acquisition of NuoEF might be reflected in the different chromosomal localization of nuoG and nuoEF in A. aeolicus (Kohlstädt et al. 2008). The inability of N7 to participate in the physiological electron transfer reaction was shown by EPR spectroscopy (Pohl et al. 2007b). The EPR difference spectrum of complex I reduced either by NADH or by dithionite revealed the signals of a tetranuclear Fe/S cluster, which were attributed to N7.
As an example, 90% of the wild type complex I activity in the membrane were restored in the strain with a chromosomal nuoB deletion complemented with pBADnuoB (Flemming et al. 2003a). Sucrose gradient centrifugation of a detergent extract of the cytoplasmic membranes of this strain revealed the presence of a stable complex I. An SDS-PAGE analysis of the preparation of complex I from this strain confirmed all complex I subunits. The enzymatic activity and EPR spectroscopic features of the presence of Fe/S clusters of the preparation were virtually identical to those of the parental strain (Flemming et al.
A Structural Perspective on Respiratory Complex I: Structure and Function of NADH:ubiquinone oxidoreductase by Rouslan G. Efremov, Leonid Sazanov (auth.), Leonid Sazanov (eds.)