Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae

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• 作者：Rizvan C. Uluisik^a ; Neval Akbas^a ; Gudrun S. Lukat-Rodgers^b ; Seth A. Adrian^b ; Courtni E. Allen^c ; Michael P. Schmitt^c ; Kenton R. Rodgers^b ; ^{Kent.Rodgers@ndsu.edu} ; Dabney W. Dixon^a ; ^{ddixon@gsu.edu}
• 关键词：ABC transporter ; ATP-binding cassette transporter ; CD ; circular dichroism ; CO ; carbon monoxide ; CR ; conserved region ; CT ; charge-transfer ; CV ; column volume ; DMSO ; dimethyl sulfoxide ; ELISA ; enzyme-linked immunosorbent assay ; ESI ; electrospray ionization ; FPLC ; fast protein liquid chromatography ; GdnHCl ; guanidinium hydrochloride ; Hb ; hemoglobin ; Hp ; haptoglobin ; HS ; high spin ; HSA ; human serum albumin ; IPTG ; isopropyl β-d-1-thiogalactopyranoside ; LS ; low-spin ; PMSF ; phenylmethanesulfonyl fluori
• 刊名：Journal of Inorganic Biochemistry
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：167
• 期：Complete
• 页码：124-133
• 全文大小：1098 K
• 卷排序：167

文摘

The heme in HtaA-CR2 is coordinated by an axial tyrosine. Mutation of the axial ligand and a potential hydrogen-bonding partner His reduced heme binding. Reconstitution of the protein after full unfolding significantly altered the heme binding pocket. HtaA-CR2 is very stable toward heat and treatment with guanidinium hydrochloride. Bound heme plays an essential role in the stability of HtaA-CR2.