histidine hydrogen-deuterium exchange mass spectrometry for probing the microenvironment of histidine residues in dihydrofolate reductase组氨酸hydrogen-deuterium交换质谱探测二氢叶酸还原酶的组氨酸残基的微环境.pdfVIP
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histidine hydrogen-deuterium exchange mass spectrometry for probing the microenvironment of histidine residues in dihydrofolate reductase组氨酸hydrogen-deuterium交换质谱探测二氢叶酸还原酶的组氨酸残基的微环境
Histidine Hydrogen-Deuterium Exchange Mass
Spectrometry for Probing the Microenvironment of
Histidine Residues in Dihydrofolate Reductase
1,2,3 . 2. 2 1 1
Masaru Miyagi * , Qun Wan , Md. Faiz Ahmad , Giridharan Gokulrangan , Sara E. Tomechko , Brad
Bennett2¤, Chris Dealwis1,2*
1 Case Center for Proteomics and Bioinformatics, Case Western Reserve University, Cleveland, Ohio, United States of America, 2 Department of Pharmacology, Case
Western Reserve University, Cleveland, Ohio, United States of America, 3 Department of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland,
Ohio, United States of America
Abstract
Background: Histidine Hydrogen-Deuterium Exchange Mass Spectrometry (His-HDX-MS) determines the HDX rates at the
imidazole C2-hydrogen of histidine residues. This method provides not only the HDX rates but also the pKa values of
histidine imidazole rings. His-HDX-MS was used to probe the microenvironment of histidine residues of E. coli dihydrofolate
reductase (DHFR), an enzyme proposed to undergo multiple conformational changes during catalysis.
Methodology/Principal Findings: Using His-HDX-MS, the pKa values and the half-lives (t1/2) of HDX reactions of five
histidine residues of apo-DHFR, DHFR in complex with methotrexate (DHFR-MTX), DHFR in complex with MTX and NADPH
(DHFR-MTX-NADPH), and DHFR in complex with folate and NADP+ +
(DHFR-folate-NADP ) were determined. The results
showed that the two parameters (pKa and t1/2) are sensitive to the changes of the microenviron
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