ArticleScientific reports2015
Structural Changes and Proton Transfer in Cytochrome c Oxidase.
Article in Scientific reports, 2015. 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, 17 citations in OpenAlex.
- Proton transfer reactions: From photochemistry to biochemistry and bioenergetics.BBA advances · 2023Article
- Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase.Scientific reports · 2019Article
- Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.Scientific reports · 2018Article
- Insights into functions of the H channel of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Crystal structure of CO-bound cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Isolation of yeast complex IV in native lipid nanodiscs.Biochimica et biophysica acta · 2016Article
- Rapid Electron Transfer within the III-IV Supercomplex in Corynebacterium glutamicum.Scientific reports · 2016Article
- Regulatory role of the respiratory supercomplex factors in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In cytochrome c oxidase electron transfer from cytochrome c to O2 is linked to transmembrane proton pumping, which contributes to maintaining a proton electrochemical gradient across the membrane. The mechanism by which cytochrome c oxidase couples the exergonic electron transfer to the endergonic proton translocation is not known, but it presumably involves local structural changes that control the alternating proton access to the two sides of the membrane. Such redox-induced structural changes have been observed in X-ray crystallographic studies at residues 423-425 (in the R. sphaeroides oxidase), located near heme a. The aim of the present study is to investigate the functional effects of these structural changes on reaction steps associated with proton pumping. Residue Ser425 was modified using site-directed mutagenesis and time-resolved spectroscopy was used to investigate coupled electron-proton transfer upon reaction of the oxidase with O2. The data indicate that the structural change at position 425 propagates to the D proton pathway, which suggests a link between redox changes at heme a and modulation of intramolecular proton-transfer rates.
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