Related Experiment Video
Updated: Aug 23, 2026

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
Published on: November 26, 2014
Structural and functional analogue of the active site of polysulfide reductase from Wolinella succinogenes
Kowliki Nagarajan1, Hemant K Joshi, Pradeep K Chaudhury
1Department of Chemistry, Indian Institute of Technology, Kanpur-208 016, India.
Abstract:
Synthesis of [PPh4]2[Mo(SPh)2(S2C2(CN)2)2] (2) from [PPh4]2[MoO(S2C2(CN)2)2] (1) has been achieved to mimic the postulated [Mo(S)6] core of polysulfide reductase with two thiolates and two bis(ene-dithiolate) ligands. Compound 2 reacts with polysulfide to yield H2S, modeling the function of polysulfide reductase. The facile conversion of 2 back to 1 in moist solvent suggests that the interconversion of the [MoIV = O] and [MoIV - X] (X = O-Ser, S-Cys, Se-Cys) moieties might occur in the DMSO reductase class of enzymes under appropriate hydrophobic/hydrophilic conditions.
Related Concept Videos
Preparation and Reactions of Sulfides
Sulfur Assimilation
Structure and Nomenclature of Thiols and Sulfides
Ligand Binding and Linkage
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
