How large is the [Fe(III)(protoporphyrin IX)]+ ion (hemin+) in the gas phase?
نویسندگان
چکیده
Comparison of the collision cross-section of the [Fe(III)-protoporphyrin IX]+ ion, hemin+, measured by means of ion-mobility experiments and the cross-sections calculated from theoretical structures based on density functional theory reveals that hemin+, in the gas phase, contains intramolecular hydrogen bonding between its two propionic acid side-chains.
منابع مشابه
Neurotrophic activity of neudesin, a novel extracellular heme-binding protein, is dependent on the binding of heme to its cytochrome b5-like heme/steroid-binding domain.
Neudesin is a secreted protein with neurotrophic activity in neurons and undifferentiated neural cells. We report here that neudesin is an extracellular heme-binding protein and that its neurotrophic activity is dependent on the binding of heme to its cytochrome b(5)-like heme/steroid-binding domain. At first, we found that at least a portion of the purified recombinant neudesin appeared to bin...
متن کاملRuffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus.
IsdG and IsdI are paralogous proteins that are intracellular components of a complex heme uptake system in Staphylococcus aureus. IsdG and IsdI were shown previously to reductively degrade hemin. Crystal structures of the apoproteins show that these proteins belong to a newly identified heme degradation family distinct from canonical eukaryotic and prokaryotic heme oxygenases. Here we report th...
متن کاملThe Enzymic Conversion of Protoporphyrinogen IX to Protoporphyrin IX
The oxidation of protoporphyrinogen IX to protoporphyrin TX in yeast cells is enzyme-dependent. The enzyme, protoporphyrinogen oxidase, associated with purified mitochondria isolated from Saccharomyces cereuisiae was solubilized by sonic treatment in the presence of detergent and partially purified. The molecular weight of the enzyme was 180,000 f 18,000. The purified preparation could be store...
متن کاملThe inhibitory effect of heme on heme formation in vivo: possible mechanism for the regulation of hemoglobin synthesis.
1) The effect of hemin on heme synthesis was studied in vivo. Heme synthesis was measured by determining red cell (59)Fe uptake and glycine-2-(14)C incorporation into red cell hemin in normal CF(1) female mice.2) Both bovine and human hemin significantly decreased red cell (59)Fe uptake 48, 72, and 96 hours after hemin injection.3) Glycine-2-(14)C incorporation into red cell hemin was decreased...
متن کاملHemin binding by Porphyromonas gingivalis strains is dependent on the presence of A‐LPS
Porphyromonas gingivalis is a Gram-negative black pigmenting anaerobe that is unable to synthesize heme [Fe(II)-protoporphyrin IX] or hemin [Fe(III)-protoporphyrin IX-Cl], which are important growth/virulence factors, and must therefore derive them from the host. Porphyromonas gingivalis expresses several proteinaceous hemin-binding sites, which are important in the binding/transport of heme/he...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The journal of physical chemistry. B
دوره 110 47 شماره
صفحات -
تاریخ انتشار 2006