Does anyone know a specific membrane-permeable MnSOD inhibitor?

I have submitted my paper to one of the springer journal. For the first week of submission, the status was "with editor" and then it changed to under review for one week, then reviewers asigned for the next two days then again changed to under review for 10 days then finally to "required reviews completed". The status reviews completed was for one week and then it changed to with editor again for last 10 days. Now my question is if it is rejection then the editor would immediately send the rejection letter. Why the editor is taking time to decide? Is it a good sign or a bad one??

I've been digging through piles and piles of literature for studies of ROS mediated control of signaling cascades - does anyone have any good article suggestions?   (feel free to toot your own horn here!)

There is a surprisingly large amount of poor or confusing info out there - I'm trying to speed my search and not get distracted by misleading studies 

I am planning to use an inhibitor for HO-1, but on doing western blot we could see HO-1 bands, I am confused if we are using inhibitor we should not see those bands? And is tin mesoprotoporphyrin or Tin protoporphyrin better inhibitor? We are planning to use it in mice.

i am following two assays for antioxidant activity one is hydrogen peroxide and ammonium molybdate but am getting negative absorbance in control or in test sample what i suppose to do now?

I'm trying to run some experiments dealing with in vitro oxidative damage, using commercial preparations of blood plasma as a representative biological medium. The assay I'm using is the ferric reducing ability of plasma (FRAP) assay. I'm trying to establish a positive control for damaged plasma. In other words, I don't want a negative control such as plain methanol or something similar i.e. the complete absence of antioxidants; I want to use plasma that had an antioxidant potential to begin with, but that I abolished or damaged using some treatment.

Originally I was trying to use hydrogen peroxide in order to oxidize the antioxidants in plasma, but today we discovered something very curious; there is a distinct positive correlation between increased concentrations of H2O2 that are being "spiked" into blood plasma, and apparent increases in FRAP from a kinetic standpoint. It sounds confusing and completely contrary to what you'd expect, but the higher the concentration of H2O2 you use in plasma, the faster and more intensely the purple colour of the (TPTZ)2-Fe2+ complex develops at 585 nm.

I was absolutely perplexed as to how this could possibly be at first, but I suppose it's due to one of the following (or a combination of the two):

a) Some sort of Fenton reaction/Haber-Weiss cycle of peroxide-treated plasma is affecting both the iron in plasma and the FeCl3 of the FRAP reagent, and making it seem as though blood plasma spiked with H2O2 has way more antioxidant potential than untreated plasma. I'm not quite sure of radical and/or redox mechanisms of this (I would have thought the iron might "cycle" between Fe3+ and Fe2+ but not remain "locked" at Fe2+), but I can't ignore the fact that increasing [H2O2] positively correlates with increasing kinetic development of the coloured complex at 585 nm;

b) The longer H2O2 is left to incubate with blood plasma, the more it is damaging plasma proteins, and causing potential release of iron from those proteins (e.g.transferrin). That said, those proteins will still bind Fe3+, not Fe2+, so the question remains of how Fe3+ is being reduced.

Whether the case is a) or b) or something else is really neither here nor there, truthfully. The *ultimate* question of all this is: is there a way to "damage" the antioxidant potential of plasma such as to establish a positive control for decreased FRAP, while having the results of the assay actually make sense?

It is well known that this amazing linear tripeptide of L-glutamine, L-cysteine, and glycine is often referred to as the body's master antioxidant. Once generation of free radicals exceeds the body's capacity to neutralize and eliminate them, oxidative stress occurs, and primary function of glutathione is to alleviate this oxidative stress. Low Glutathione levels are associated with health diseases such as Cancer, Multiple Sclerosis, AIDS, Alzheimer’s, Parkinson’s, Atherosclerosis, Pregnancy Complications, Cataracts, Asthma, Autism, Bronchitis, Fibromyalgia, Insomnia, Male infertility, Migraines, Osteoporosis, Pain, Poor Eyesight, PMS, Psoriasis, Wrinkles, Low Sex Drive, Chronic Fatigue, Balding and Cirrhosis. So can inhibition of GSH breakdown in the stomach or a induction of GSH synthesis be a step towards the fountain of youth?

Has anyone concluded that inhibiting GST (ie, with ethacrynic acid) and/or decreasing GSH (ie, with BSO) aides selection of cys-targeted covalent inhibitors?

Is dihydroethedine a reliable method? What are its applications and limitations?

I have detected ROS (reactive oxygen species) molecules using DCDHF-DA dye in yeast cells. I found that the entire cell is not glowing and the maximum intensity was at the cell periphery. Also, I could fix these ROS molecules (I mean I got same fluorescence pattern that I got after DHF staining of live cells, cells were subjected to formaldehyde fixation and processed with alcohol), and this accumulation of ROS is not toxic to cell (viability check). I hope ROS is involved in some signalling.

However, I have a doubt whether these ROS molecules are associated with a membrane or its associated proteins. If it's associated to proteins, is DHF able to detect them? As these ROS are not toxic to the cell, how do I prove the role of ROS in signaling?