Abstract:
:The clinical disorder of recessive congenital methemoglobinemia (RCM, OMIN 250800) is associated with mutations in NADH:cytochrome b5 reductase (cb5r) and manifests as cyanosis from birth. Screening a cyanotic infant indicated elevated methemoglobin levels and decreased cb5r activity suggesting RCM. Sequencing the DIA1 gene encoding cb5r revealed a novel mutation, C27161T (NCBI accession number: NT_011520), resulting in replacement of proline at amino acid 275 with leucine (P275L). To understand how this mutation would affect cb5r's function, the P275L variant was expressed in a heterologous expression system and spectroscopic, thermodynamic, and thermostability studies were performed. The leucine substitution at residue 275 was found to significantly decrease the affinity towards the physiological reducing substrate, NADH, without affecting the activity of the P275L variant. From the rat model, residue 275 is predicted to be part of a conserved "CGPPPM" motif important for the binding and correct positioning of the NADH reducing substrate. Thus P275 influences the interaction with NADH which was confirmed by the change in affinity towards the physiological reducing substrate.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Percy MJ,Crowley LJ,Boudreaux J,Barber MJdoi
10.1016/j.abb.2005.12.015subject
Has Abstractpub_date
2006-03-01 00:00:00pages
59-67issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(05)00518-7journal_volume
447pub_type
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