期刊
FEBS LETTERS
卷 582, 期 23-24, 页码 3494-3500出版社
WILEY
DOI: 10.1016/j.febslet.2008.09.018
关键词
Bacterial hemoglobin; Ligand binding; Vitreoscilla hemoglobin; Flavohemoglobin; Proximal heme site; Distal heme site; Molecular modeling
资金
- DST, India
- NSF USA (OISE422555)
- CSIR, India
Although Vitreoscilla hemoglobin (VHb) carries a conventional globin fold, its proximal site geometry is unique in having a hydrogen-bonding network between proximal site residues, HisF8-TyrG5-GluH23 and TyrG5-TyrH12. TyrG5 and TyrH12 were mutated to study their relevance in VHb function. VHb G5 mutants (Tyr95Phe and Tyr95Leu showed no stable oxyform and nitric oxide dioxygenase activity, whereas, VHb H12 mutants (Tyr126Phe and Tyr126Leu) displayed little change in their oxygen affinity indicating a crucial role of Tyr95 in protein function. The VHb H12 mutant, Tyr126Leu, enhanced the intracellular pool of oxygen and cell growth better than VHb. Molecular modeling suggests that the replacement of tyrosine with leucine in Tyr126Leu creates an opening on the protein surface that may facilitate oxygen diffusion and accumulation.
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