A5061231256- Hemoglobin structure and function
- Heme Oxygenase-1 and Carbon Monoxide
- Neonatal Health and Biochemistry
- Porphyrin and Phthalocyanine Chemistry
- Cannabis and Cannabinoid Research
- Analytical Chemistry and Chromatography
- Advanced biosensing and bioanalysis techniques
- Protein purification and stability
- Erythrocyte Function and Pathophysiology
- DNA and Nucleic Acid Chemistry
- Photosynthetic Processes and Mechanisms
- Protein Structure and Dynamics
- RNA Interference and Gene Delivery
Saint Louis University
2021-2025
AbbVie (United States)
2025
HupZ is an expected heme degrading enzyme in the acquisition and utilization pathway Group A Streptococcus. The isolated protein containing a C-terminal V5-His6 tag exhibits weak degradation activity. Here, we revisited characterized HupZ-V5-His6 via biochemical, mutagenesis, quaternary structure, UV–vis, EPR, resonance Raman spectroscopies. results show that ferric heme-protein complex did not display EPR signal binding to triggered formation of higher oligomeric states. We found was...
The UV-vis absorption, Raman imaging, and resonance (rR) spectroscopy methods were employed to study cyanohemoglobin (HbCN) adducts inside living functional red blood cells (RBCs). cyanide ligands are especially optically sensitive probes of the active site environment heme proteins. rR studies HbCN its isotopic analogues (13CN-, C15N-, 13C15N-), as well a careful deconvolution spectral data, revealed that ν(Fe-CN) stretching, δ(Fe-CN) bending, ν(C≡N) stretching modes occur at 454, 382, 2123...
Human heme oxygenase (hHO-1) is a physiologically important enzyme responsible for free catabolism. The enzyme's high regiospecificity controlled by the distal site hydrogen bond network that involves water molecules and D140 amino acid residue. In this work, we probe active environment of wild-type (WT) hHO-1 its mutants using resonance Raman (rR) spectroscopy. Cyanide ligands are more stable than dioxygen adducts an effective proteins. inherently linear geometry Fe–C–N fragment can be...