ArticlePhotosynthesis research2010
Heliobacterial Rieske/cytb complex.
Article in Photosynthesis research, 2010. 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, 21 citations in OpenAlex.
- Article
- Deletion of the cytochrome bc complex from Heliobacterium modesticaldum results in viable but non-phototrophic cells.Photosynthesis research · 2021Article
- Emergence of cytochrome bc complexes in the context of photosynthesis.Physiologia plantarum · 2017Article
- Structural analysis of diheme cytochrome c by hydrogen-deuterium exchange mass spectrometry and homology modeling.Biochemistry · 2014Article
- The molecular evolution of the Qo motif.Genome biology and evolution · 2014Article
- The Q cycle of cytochrome bc complexes: a structure perspective.Biochimica et biophysica acta · 2011Review
- Carbon flow of heliobacteria is related more to clostridia than to the green sulfur bacteria.The Journal of biological chemistry · 2010Article
- The "green" phylogenetic clade of Rieske/cytb complexes.Photosynthesis research · 2010Article
- Evolution of cytochrome bc complexes: from membrane-anchored dehydrogenases of ancient bacteria to triggers of apoptosis in vertebrates.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Data on structure and function of the Rieske/cytb complex from Heliobacteria are scarce. They indicate that the complex is related to the b (6) f complex in agreement with the phylogenetic position of the organism. It is composed of a diheme cytochrome c, and a Rieske iron-sulfur protein, together with transmembrane cytochrome b (6) and subunit IV. Additional small subunits may be part of the complex. The cofactor content comprises heme c (i), first discovered in the Q(i) binding pocket of b (6) f complexes. The redox midpoint potentials are more negative than in b (6) f complex in agreement with the lower redox midpoint potentials (by about 150 mV) of its reaction partners, menaquinone, and cytochrome c (553). The enzyme is implicated in cyclic electron transfer around the RCI. Functional studies are favored by the absence of antennae and the simple photosynthetic reaction chain but are hampered by the high oxygen sensitivity of the organism, its chlorophyll, and lipids.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.