Understanding peroxynitrite biochemistry and its potential for treating human diseases

Abstract

It is a great pleasure to see these major contributions on peroxynitrite biochemistry to be collected in this series and to be permitted to share a few biased observations here. The Archives of Biochemistry and Biophysics played a major role at a critical junction in my scientific career in 1992. For over a year, our work had been rejected after lengthy review times by Science, Nature and the Journal of Biological Chemistry. In contrast, the editors of Archives allowed us to publish a series of five papers that established peroxynitrite as a biological oxidant, showed how tyrosine nitration can be used to quantify peroxynitrite production and demonstrated that peroxynitrite was quite toxic to bacteria(–5). The reviews from Archives were insightful rather than being judgmental as to whether the results were of sufficient interest. Rafael Radi has a similar experience with his Archives paper on the iron-independent oxidation of lipids induced by peroxynitrite (6). While judged “not of sufficient interest for the readers“ of journal X, the paper has now been cited over 1200 times. By having the space to fully describe the experimental work rather than being confined to cryptic footnotes, these papers has have received many more citations than other papers that my group has published in high profile journals. Journals such as Archives play an important role in allowing new hypotheses and data to be published of which the importance is not immediately recognized by journals focused on high impact. Access over the web such as by Pubmed gives equal exposure around the world. For new investigators, the difference in where you publish on your career may not be as great as you fear and the benefits of more fully explaining your research in multiple papers in the long run will carry greater weight.

Figure 1

Nitrophenol turns yellow upon ionization at pH’s above 7.5. The biological implications for tyrosine nitration are significant, because nitrotyrosine will turn a hydrophobic residue into a more water soluble negatively charged amino acid at neutral pH.