Heike Meyer finished her Master studies in 2018 at the Institute of Biology of the Albert-Ludwigs-University in Freiburg (Germany) with the main focus on microbiology and biochemistry. This February she started her PhD in the group of Prof. Dr. Gunhild Layer at the Institute of Pharmaceutical Sciences of the University of Freiburg. She presented her work on the functional characterization of the Radical SAM enzyme NirJ, which is involved in heme d 1 biosynthesis. Heme d 1 , a tetrapyrrole with a central iron ion, contains two unusual keto groups at rings A and B. It occurs as one of the cofactors of the dissimilatory cytochrome cd 1 nitrite reductase NirS. Its biosynthesis was elucidated in recent years, except the chemically challenging introduction of both keto groups. The Radical SAM enzyme NirJ might be a possible candidate for this particular reaction. NirJ catalyzes the removal of the two propionate side chains at rings A and B. However, it is unknown whether NirJ is also responsible for the subsequent introduction of the two carbonyl groups. The presented work provided insight in the functional characterization of NirJ, as well as the challenges which needed to be overcome under anaerobic conditions. Reference: The Radical SAM enzyme NirJ catalyzes the removal of two propionate side chains during heme d 1 biosynthesis, L. Boss, R. Oehme, S. Billig, C. Birkemeyer, G. Layer, The FEBS Journal 2017, 284, 4314–4327.
Amanda Lyn Robinson obtained her MS degree in chemistry with a focus on biomolecular chemsitry as part of the Frontiers in Chemistry (FrInCh) program, shared between Paris Descartes and Paris Diderot Universities. She is now a PhD student at Paris Sud University, working under the supervision of Dr. Jean-Noël Rebilly and Pr. Frédéric Banse in the Laboratoire de Chimie Inorganique (LCI) at the Institut de Chimie Moléculaire et des Matériaux d’Orsay (ICMMO). Her main research interests include biomimetic chemistry and small molecule activation. At the French BIC Met Bio summer school, she presented her initial results in a work entitled “A New Iron Complex with a Smart Second Coordination Sphere for Bioinspired Oxidation Catalysis.” These results were the first part of an ongoing investigation of a novel iron complex that mimics key aspects of the cytochrome P450 enzyme.
Martha Zoumpoulaki got her MS degree in Molecular Chemistry and Chemical Biology at Sorbonne Université in 2017 (M2 Chimie Moléculaire Program), in parallel with the diploma of the Ecole Normale Supérieure of Paris with a major in chemistry and a minor in theatre studies. She is now a PhD student in Laboratoire des Biomolecules (LBM) and her fellowship is funded by the ANR. She works with Clotilde Policar and Nicolas Delsuc at Laboratoire des Biomolecules (LBM) in collaboration with Joelle Vinh at the Biological Mass Spectrometry and Proteomics lab (SMBP) at the ESPCI. She presented her work entitled: Quantifying the cellular redoxome: Effect of a MnSOD mimic, a potential metallodrug against Inflammatory Bowel Diseases. A Mn-complex with a superoxide dismutase activity (Mn1) was studied in a cellular model of oxidative stress and inflammation. It was previously shown to have an intracellular anti-superoxide and anti-inflammatory activity 1 . This work describes the use of a metabolic labeling strategy to quantify the effect of Mn1 on the expression levels of proteins and the redox state of cysteines using LC-MS/MS. Mathieu E. et al., Inorg. Chem 2017, 56, 5, 2555