in the present study, we investigated the effect of a new anticancer pd(ii) complex, 1,10-phenanthroline-n-butyl dithiocarbamato pd(ii) nitrate, on the heme releasing from human hemoglobin (hb) as well as alterations in the structure and function of hb using different spectroscopic methods of uv-vis, fluorescence and circular dichroism (cd)at two temperatures of 25 and 37 °c. fluorescence data ...

The eukaryotic heme oxygenases (HOs) (E.C. 1.14.99.3) convert heme to biliverdin, iron, and carbon monoxide (CO) in three successive oxygenation steps. Pathogenic bacteria require iron for survival and infection. Extracellular heme uptake from the host plays a critical role in iron acquisition and virulence. In the past decade, several HOs required for the release of iron from extracellular hem...

In the present study, we investigated the effect of a new anticancer Pd(II) complex, 1,10-phenanthroline-n-butyl dithiocarbamato Pd(II) nitrate, on the heme releasing from human hemoglobin (Hb) as well as alterations in the structure and function of Hb using different spectroscopic methods of UV-Vis, fluorescence and circular dichroism (CD)at two temperatures of 25 and 37 °C. Fluorescence data ...

The transcription repressor Bach1 is a sensor and effector of heme that regulates the expression of heme oxygenase 1 and globin genes. Heme binds to Bach1, inhibiting its DNA binding activity and inducing its nuclear export. We found that hemin further induced the degradation of endogenous Bach1 in NIH 3T3 cells, murine embryonic fibroblasts, and murine erythroleukemia cells. In contrast, succi...

Splenic red pulp macrophages (RPM) degrade senescent erythrocytes and recycle heme-associated iron. The transcription factor SPI-C is selectively expressed by RPM and is required for their development, but the physiologic stimulus inducing Spic is unknown. Here, we report that Spic also regulated the development of F4/80(+)VCAM1(+) bone marrow macrophages (BMM) and that Spic expression in BMM a...

Iron-regulatory proteins (IRPs) recognize and bind to specific RNA structures called iron-responsive elements. Mediation of these binding interactions by iron and iron-containing compounds regulates several post-transcriptional events relevant to iron metabolism. There are two known IRPs, IRP1 and IRP2, both of which can respond to iron fluxes in the cell. There is ample evidence that IRP1 is c...

TSPO, a stress-induced, posttranslationally regulated, early secretory pathway-localized plant cell membrane protein, belongs to the TspO/MBR family of regulatory proteins, which can bind porphyrins. This work finds that boosting tetrapyrrole biosynthesis enhanced TSPO degradation in Arabidopsis thaliana and that TSPO could bind heme in vitro and in vivo. This binding required the His residue a...

TSPO, a stress-induced, posttranslationally regulated, early secretory pathway-localized plant cell membrane protein, belongs to the TspO/MBR family of regulatory proteins, which can bind porphyrins. This work finds that boosting tetrapyrrole biosynthesis enhanced TSPO degradation in Arabidopsis thaliana and that TSPO could bind heme in vitro and in vivo. This binding required the His residue a...

The conversion of endogenous hepatic heme to bilirubin and CO is established. However, it is unknown whether this process is quantitative or whether heme may be degraded to other products as well. To study this question, we administered the heme precursor, delta-amino-[5-14C]levulinic acid to rats in vivo. In liver, [14C]heme was predominately associated with microsomal cytochromes, and its deg...

Hematin, the drug used for acute porphyric attacks, has been shown to cause disturbances in hemostasis, mainly because of its degradation products. Lately a new heme compound, heme arginate, has been developed for the treatment of porphyrias. In experimental animal studies as well as in clinical use it has proved to be well tolerated. To find out whether heme arginate has any effects on hemosta...