Open AccessBook
Organic sulfur compounds
N. Kharasch,John T. Zimmer +1 more
About:
The article was published on 1961-01-01 and is currently open access. It has received 293 citations till now. The article focuses on the topics: Metal sulfur dioxide complex & Sulfur.read more
Citations
More filters
Journal ArticleDOI
The chemical diversity and distribution of glucosinolates and isothiocyanates among plants
TL;DR: This review addresses the complex array of glucosinolates, the precursors of isothiocyanates, present in sixteen families of dicotyledonous angiosperms including a large number of edible species including Brassica vegetables.
Journal ArticleDOI
A Critical Review of the Literature on Hydrogen Sulfide Toxicity
TL;DR: This review of the literature is intended as an evaluative report rather than an annotated bibliography of all the source material examined on hydrogen sulfide, noting information gaps that may require further investigation.
Journal ArticleDOI
Pristine graphite oxide.
TL;DR: It is shown that the structure and properties of GO depend significantly on the quenching and purification procedures, rather than, as is commonly thought, on the type of graphite used or oxidation protocol, which allows us to add critical details to existing GO models.
Journal ArticleDOI
Cycling of volatile organic sulfur compounds in anaerobically digested biosolids and its implications for odors.
Matthew J. Higgins,Yen-Chih Chen,Douglas P. Yarosz,Sudhir Murthy,Nick A. Maas,Dietmar Glindemann,John T. Novak +6 more
TL;DR: The research demonstrated that the main source of VOSCs was the biodegradation of protein within the biosolids and the results provided a framework for understanding the production of odor from anaerobically digested sludges before and after dewatering.
Book ChapterDOI
Sulfhydryl Groups in Membrane Structure and Function
TL;DR: The sulfhydryl group not only constitutes a unique marker for delineating the general role of proteins in membrane functions, it can also serve as a marker for specific functional proteins through the use of radioactive reagents that form stable bonds with sulfHydryls.