scholarly journals Cover Feature: Coculturing of Mosquito‐Microbiome Bacteria Promotes Heme Degradation in Elizabethkingia anophelis (ChemBioChem 9/2020)

ChemBioChem ◽  
2020 ◽  
Vol 21 (9) ◽  
pp. 1234-1234
Author(s):  
Jack G. Ganley ◽  
Hannah K. D'Ambrosio ◽  
Meg Shieh ◽  
Emily R. Derbyshire
Keyword(s):  
Heme Degradation

scholarly journals Heme Binding to HupZ with a C-Terminal Tag from Group A Streptococcus

Molecules ◽  
2021 ◽  
Vol 26 (3) ◽  
pp. 549
Author(s):  
Ephrahime S. Traore ◽  
Jiasong Li ◽  
Tapiwa Chiura ◽  
Jiafeng Geng ◽  
Ankita J. Sachla ◽  
...  
Keyword(s):  
Quaternary Structure ◽  
Group A Streptococcus ◽  
Heme Binding ◽  
Oligomeric Structure ◽  
Heme Degradation ◽  
Group A ◽  
Degradation Activity ◽  
Ferric Heme ◽  
Epr Signal ◽  
Utilization Pathway

HupZ is an expected heme degrading enzyme in the heme acquisition and utilization pathway in Group A Streptococcus. The isolated HupZ protein containing a C-terminal V5-His6 tag exhibits a weak heme degradation activity. Here, we revisited and characterized the HupZ-V5-His6 protein via biochemical, mutagenesis, protein quaternary structure, UV–vis, EPR, and resonance Raman spectroscopies. The results show that the ferric heme-protein complex did not display an expected ferric EPR signal and that heme binding to HupZ triggered the formation of higher oligomeric states. We found that heme binding to HupZ was an O2-dependent process. The single histidine residue in the HupZ sequence, His111, did not bind to the ferric heme, nor was it involved with the weak heme-degradation activity. Our results do not favor the heme oxygenase assignment because of the slow binding of heme and the newly discovered association of the weak heme degradation activity with the His6-tag. Altogether, the data suggest that the protein binds heme by its His6-tag, resulting in a heme-induced higher-order oligomeric structure and heme stacking. This work emphasizes the importance of considering exogenous tags when interpreting experimental observations during the study of heme utilization proteins.

scholarly journals Suppression of hyperbilirubinemia in the rat neonate by chromium-protoporphyrin. Interactions of metalloporphyrins with microsomal heme oxygenase of human spleen.

1982 ◽  
Vol 156 (6) ◽  
pp. 1878-1883 ◽  
Author(s):  
G S Drummond ◽  
A Kappas
Keyword(s):  
Single Dose ◽  
Heme Oxygenase ◽  
Competitive Inhibitor ◽  
Bile Pigment ◽  
Human Spleen ◽  
Oxidation Activity ◽  
Heme Oxygenase Activity ◽  
Heme Degradation ◽  
Oxygenase Activity ◽  
Liver And Kidney

The synthetic metalloporphyrin, Cr-protoporphyrin, as a potent competitive inhibitor of heme oxygenase activity in rat spleen, liver, and kidney. When administered to neonatal animals in a single dose immediately after birth, Cr-protoporphyrin suppresses postnatal hyperbilirubinemia and produces a marked and sustained lowering of heme oxidation activity in liver, spleen, and kidney. The metalloporphyrin also potently inhibited the rate of heme degradation to bile pigment in human spleen.

Nitrite attenuated hypochlorous acid-mediated heme degradation in hemoglobin

2015 ◽  
Vol 238 ◽  
pp. 25-32 ◽  
Author(s):  
Naihao Lu ◽  
Jiayu Li ◽  
Xiaoming Ren ◽  
Rong Tian ◽  
Yi-Yuan Peng
Keyword(s):  
Hypochlorous Acid ◽  
Heme Degradation

Site-Specific Cross-Linking of Human and Bovine Hemoglobins Differentially Alters Oxygen Binding and Redox Side Reactions Producing Rhombic Heme and Heme Degradation†

Biochemistry ◽  
2002 ◽  
Vol 41 (23) ◽  
pp. 7407-7415 ◽  
Author(s):  
Enika Nagababu ◽  
Somasundaram Ramasamy ◽  
Joseph Moses Rifkind ◽  
Yiping Jia ◽  
Abdu I. Alayash
Keyword(s):  
Cross Linking ◽  
Side Reactions ◽  
Oxygen Binding ◽  
Site Specific ◽  
Heme Degradation

scholarly journals 922 THE INHIBITORY EFFECT OF TIN PROTOPORPHYRIN (SN-P) ON HEME DEGRADATION

1985 ◽  
Vol 19 (4) ◽  
pp. 264A-264A ◽  
Author(s):  
Stephen Landaw ◽  
Shiqeru Sassa ◽  
George Drummond ◽  
Attallah Kappas
Keyword(s):  
Inhibitory Effect ◽  
Heme Degradation ◽  
Tin Protoporphyrin

ROS-mediated heme degradation and cytotoxicity induced by iron nanoparticles: hemoglobin and lymphocyte cells as targets

2017 ◽  
Vol 36 (16) ◽  
pp. 4235-4245 ◽  
Author(s):  
Sepideh Mirzaei ◽  
Zari Hadadi ◽  
Farnoosh Attar ◽  
Seyyedeh Elaheh Mousavi ◽  
Seyed Shahaboddin Zargar ◽  
...  
Keyword(s):  
Iron Nanoparticles ◽  
Heme Degradation

Heme degradation and iron release of hemoglobin and oxidative stress of lymphocyte cells in the presence of silica nanoparticles

2018 ◽  
Vol 118 ◽  
pp. 800-807 ◽  
Author(s):  
Samaneh Azimipour ◽  
Samaneh Ghaedi ◽  
Zahra Mehrabi ◽  
Seyed Ali Ghasemzadeh ◽  
Masoumeh Heshmati ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Silica Nanoparticles ◽  
Iron Release ◽  
Heme Degradation ◽  
And Oxidative Stress

scholarly journals The Heme Degradation Pathway is a Promising Serum Biomarker Source for the Early Detection of Alzheimer's Disease

2010 ◽  
Vol 19 (3) ◽  
pp. 1081-1091 ◽  
Author(s):  
Claudius Mueller ◽  
Weidong Zhou ◽  
Amy VanMeter ◽  
Michael Heiby ◽  
Shino Magaki ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Early Detection ◽  
Degradation Pathway ◽  
Serum Biomarker ◽  
Heme Degradation
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