ArticlePloS one2016
Evidence for Fast Electron Transfer between the High-Spin Haems in Cytochrome bd-I from Escherichia coli.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Bioenergetics and Reactive Nitrogen Species in Bacteria.International journal of molecular sciences · 2022Review
- Recent Advances in Structural Studies of CytochromeInternational journal of molecular sciences · 2022Review
- Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics.International journal of molecular sciences · 2021Review
- Proton Pumping and Non-Pumping Terminal Respiratory Oxidases: Active Sites Intermediates of These Molecular Machines and Their Derivatives.International journal of molecular sciences · 2021Review
- Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021Review
- Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Biphenyl Modulates the Expression and Function of Respiratory Oxidases in the Polychlorinated-Biphenyls DegraderFrontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Cytochrome bd-I is one of the three proton motive force-generating quinol oxidases in the O2-dependent respiratory chain of Escherichia coli. It contains one low-spin haem (b558) and the two high-spin haems (b595 and d) as the redox-active cofactors. In order to examine the flash-induced intraprotein reverse electron transfer (the so-called ''electron backflow''), CO was photolyzed from the ferrous haem d in one-electron reduced (b5583+b5953+d2+-CO) cytochrome bd-I, and the fully reduced (b5582+b5952+d2+-CO) oxidase as a control. In contrast to the fully reduced cytochrome bd-I, the transient spectrum of one-electron reduced oxidase at a delay time of 1.5 μs is clearly different from that at a delay time of 200 ns. The difference between the two spectra can be modeled as the electron transfer from haem d to haem b595 in 3-4% of the cytochrome bd-I population. Thus, the interhaem electron backflow reaction induced by photodissociation of CO from haem d in one-electron reduced cytochrome bd-I comprises two kinetically different phases: the previously unnoticed fast electron transfer from haem d to haem b595 within 0.2-1.5 μs and the slower well-defined electron equilibration with τ ~16 μs. The major new finding of this work is the lack of electron transfer at 200 ns.
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Registered trials
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