Abstract：
:HtaA is a heme-binding protein that is part of the heme uptake system in Corynebacterium diphtheriae. HtaA contains two conserved regions (CR1 and CR2). It has been previously reported that both domains can bind heme; the CR2 domain binds hemoglobin more strongly than the CR1 domain. In this study, we report the biophysical characteristics of HtaA-CR2. UV-visible spectroscopy and resonance Raman experiments are consistent with this domain containing a single heme that is bound to the protein through an axial tyrosine ligand. Mutants of conserved tyrosine and histidine residues (Y361, H412, and Y490) have been studied. These mutants are isolated with very little heme (≤5%) in comparison to the wild-type protein (~20%). Reconstitution after removal of the heme with butanone gave an alternative form of the protein. The HtaA-CR2 fold is very stable; it was necessary to perform thermal denaturation experiments in the presence of guanidinium hydrochloride. HtaA-CR2 unfolds extremely slowly; even in 6.8M GdnHCl at 37°C, the half-life was 5h. In contrast, the apo forms of WT HtaA-CR2 and the aforementioned mutants unfolded at much lower concentrations of GdnHCl, indicating the role of heme in stabilizing the structure and implying that heme transfer is effected only to a partner protein in vivo.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Uluisik RC,Akbas N,Lukat-Rodgers GS,Adrian SA,Allen CE,Schmitt MP,Rodgers KR,Dixon DWdoi
10.1016/j.jinorgbio.2016.11.027subject
Has Abstractpub_date
2017-02-01 00:00:00pages
124-133eissn
0162-0134issn
1873-3344pii
S0162-0134(16)30430-5journal_volume
167pub_type
杂志文章abstract：:In this work we report a series of Cu(II) complexes [Cu(N-N)2(X)]+, (N-N=substituted 1,10-phenanthroline derivatives and X=Cl- or NO3-), with tunable E1/2 for electrochemical reduction [CuII(N-N)2(X)]++1e-⇌[CuI(N-N)2]+X-. The disproportion of O2•- was explored in presence of the electro-generated species [CuI(N-N)2]+ ...
journal_title：Journal of inorganic biochemistry
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journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
doi：10.1016/j.jinorgbio.2006.07.013
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pub_type： 杂志文章
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更新日期：2005-09-01 00:00:00
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doi：10.1016/0162-0134(95)00005-9
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journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
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doi：10.1016/j.jinorgbio.2010.03.007
更新日期：2010-07-01 00:00:00
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更新日期：2018-09-01 00:00:00
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journal_title：Journal of inorganic biochemistry
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更新日期：2016-09-01 00:00:00
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journal_title：Journal of inorganic biochemistry
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journal_title：Journal of inorganic biochemistry
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journal_title：Journal of inorganic biochemistry
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journal_title：Journal of inorganic biochemistry
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更新日期：2009-05-01 00:00:00
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journal_title：Journal of inorganic biochemistry
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更新日期：2009-07-01 00:00:00
abstract：:Polyoxometalates (POMs) are promising inorganic inhibitors for P-type ATPases. The experimental models used to study the effects of POMs on these ATPases are usually in vitro models using vesicles from several membrane sources. Very recently, some polyoxotungstates, such as the Dawson anion [P2W18O62]6-, were shown to...
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更新日期：2019-08-01 00:00:00
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journal_title：Journal of inorganic biochemistry
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abstract：:The title compound ([3,5-Me(2)bpzaH(2)][AuCl(4)]Cl, 1) (Me(2)bpza=bis(3,5-dimethylpyrazolyl)acetic acid), was prepared by reacting H[AuCl(4)] with 3,5-Me(2)bpza; and spectroscopically and structurally characterized. In the solid state structure of 1, the pyrazolyl ligand is doubly protonated to form two strong charge ...
journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
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更新日期：2009-02-01 00:00:00
abstract：:Iron deficiency anemia is a relatively common illness that can arise from a number of different causes. Three ferrous salts are usually used in its treatment: ferrous fumarate, gluconate, and sulfate. They are administered orally and are relatively well tolerated. These hematinics have been studied by Mössbauer spectr...
journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
doi：10.1016/0162-0134(94)00062-f
更新日期：1995-06-01 00:00:00
