ArticleGenome biology and evolution2015
Genome Analysis of Structure-Function Relationships in Respiratory Complex I, an Ancient Bioenergetic Enzyme.
Article in Genome biology and evolution, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Conditional essentiality of the 11-subunit complex I-like enzyme in strict anaerobes: the case ofFrontiers in microbiology · 2024Article
- New Insights on Rotenone Resistance of Complex I Induced by the m.11778G>A/Molecules (Basel, Switzerland) · 2022Article
- New Alphaproteobacteria Thrive in the Depths of the Ocean with Oxygen Gradient.Microorganisms · 2022Article
- Structure of inhibitor-bound mammalian complex I.Nature communications · 2020Article
- Effectiveness of nitrogen fixation in rhizobia.Microbial biotechnology · 2020Review
- Complex I and II Subunit Gene Duplications Provide Increased Fitness to Worms.Frontiers in genetics · 2019Article
- Burrowers from the Past: Mitochondrial Signatures of Ordovician Bivalve Infaunalization.Genome biology and evolution · 2017Article
- The functional microbiome of arthropods.PloS one · 2017Article
- Alpha proteobacterial ancestry of the [Fe-Fe]-hydrogenases in anaerobic eukaryotes.Biology direct · 2016Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a ubiquitous bioenergetic enzyme formed by over 40 subunits in eukaryotes and a minimum of 11 subunits in bacteria. Recently, crystal structures have greatly advanced our knowledge of complex I but have not clarified the details of its reaction with ubiquinone (Q). This reaction is essential for bioenergy production and takes place in a large cavity embedded within a conserved module that is homologous to the catalytic core of Ni-Fe hydrogenases. However, how a hydrogenase core has evolved into the protonmotive Q reductase module of complex I has remained unclear. This work has exploited the abundant genomic information that is currently available to deduce structure-function relationships in complex I that indicate the evolutionary steps of Q reactivity and its adaptation to natural Q substrates. The results provide answers to fundamental questions regarding various aspects of complex I reaction with Q and help re-defining the old concept that this reaction may involve two Q or inhibitor sites. The re-definition leads to a simplified classification of the plethora of complex I inhibitors while throwing a new light on the evolution of the enzyme function.
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Registered trials
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