I have been working on formate dehydrogenase (oxidoreductase) and found that most of them are oxygen liable. I have done some literature review to know the role of some co factors behind this property but did not figure out the exact reason behind this. It would be great if anyone help me finding the structural requirement for the oxygen tolerance of formate dehydrogenase.
Dear Dr Pradeep,
One chemical red/ox reaction involves two electron reaction. In an enzyme reaction catalyzed by a heme protein, the heme can transfer only one electron at once. In case of ferri-cytochrome b reaction, the heme takes one electron either from the cofactor, sometimes from the substrate. Consequently, one-electron-reduced compound, a radical, exists in the reaction. This radical compound could be reactive to oxygen. In some occasion such as insufficient substrate supply, the radical could react to oxygen.
A review by Stuehr on NOS uncoupling may be insightful for your question.
http://www.ncbi.nlm.nih.gov/pubmed/11279231?dopt=Citation
I used to demonstrate why superoxide was produced in this kind of two step reaction, oxidation of tetrahydrobiopterin BH4 to dihydrobiopterin BH2 by ferri-cytochrome c, under aerobic conditions. In the absence of dioxygen, BH4 reduces exactly 2 molecules of ferri-cytochrome c.
http://www.ncbi.nlm.nih.gov/pubmed/214425
I hope they would be suggestive to your question.
Hiro
Dear Dr. Hiroyuki,
Thank you very much for your information. Actually, I want to know the primary, or secondary, or tertiary structural differences between the available oxygen tolerant and liable formate dehydrogenase. I have a big confusion on the difference in their structure. However, I found that oxygen tolerant FDH have similar nucleotide sequence with each other but differs hugely with liable FDH.
Thanks.
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