Structure-function studies of the Vitreoscilla hemoglobin D-region
- Authors
- Lee SY; Stark BC; Webster DA
- Issue Date
- Apr-2004
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- heme-protein interactions; bacterial hemoglobin; flavin domain; hemoglobin-flavoprotein interactions
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.316, no.4, pp.1101 - 1106
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 316
- Number
- 4
- Start Page
- 1101
- End Page
- 1106
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/86839
- DOI
- 10.1016/j.bbrc.2004.02.154
- ISSN
- 0006-291X
- Abstract
- The D-region connecting helices C and E of Vitreoscilla hemoglobin (VHb) appears disordered in the crystal structure. Six site-directed mutants in this region were made to investigate its possible functions. The mutant VHb's were analyzed using UV-visible and FTIR spectroscopy, using primarily the CO liganded forms, and their heme/protein ratios were determined. The results implicate Asp44, Arg47. and Glu49 as especially important in heme-globin interactions and ligand binding, and enabled construction of a model in which the D-region forms a loop that protrudes upward over the heme. Interactions between VHb (wild type and the D-region mutants) with the flavin domain of 2,4-DNT dioxygenase from Burkholderia were tested using bacterial two-hybrid screening. There was a correlation between the extent of the D-loop perturbation predicted for each mutant and the amount of the reduction in VHb-flavin domain interaction, suggesting that this region may be more generally involved in binding of VHb to flavoproteins. (C) 2004 Elsevier Inc. All rights reserved.
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