Evaluation of relative contributions of two enzymes supposed to metabolise hydrogen peroxide in Paracoccus denitrificans
Biochimica et Biophysica Acta (BBA) - Bioenergetics, ISSN: 0005-2728, Vol: 1410, Issue: 1, Page: 71-76
1999
- 5Citations
- 10Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations5
- Citation Indexes5
- CrossRef5
- Captures10
- Readers10
- 10
Article Description
A biosensor exploiting an electrochemically mediated enzyme-catalysed reaction was used to quantify relative contributions of cytoplasmic catalase and periplasmic cytochrome c peroxidase to the overall rate of hydrogen peroxide breakdown in cells of Paracoccus denitrificans. The effects of antimycin (an inhibitor of electron flow to cytochrome c peroxidase), the reaction rate versus substrate concentration profiles for the whole cells and subcellular fractions, and the time courses of oxygen concentration demonstrated a profound decrease in the capacity of cytochrome c peroxidase to reduce H 2 O 2 under in vivo conditions. The reason is suggested to be a competition for available electrons between the enzyme and terminal oxidases metabolising oxygen produced by catalase.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0005272898001765; http://dx.doi.org/10.1016/s0005-2728(98)00176-5; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0344958667&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10076016; http://linkinghub.elsevier.com/retrieve/pii/S0005272898001765; http://api.elsevier.com/content/article/PII:S0005272898001765?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0005272898001765?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0005272898001765; http://dx.doi.org/10.1016/s0005-2728%2898%2900176-5
Elsevier BV
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