Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM032696-08S1
Application #
3281744
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1984-09-27
Project End
1996-08-31
Budget Start
1992-09-01
Budget End
1993-08-31
Support Year
8
Fiscal Year
1993
Total Cost
Indirect Cost

  Institution

Name
University of South Florida
Department
Type
Schools of Medicine
DUNS #
City
Tampa
State
FL
Country
United States
Zip Code
33612

  Publications

Percy, M J; Crowley, L J; Boudreaux, J et al. (2006) Expression of a novel P275L variant of NADH:cytochrome b5 reductase gives functional insight into the conserved motif important for pyridine nucleotide binding. Arch Biochem Biophys 447:59-67
Percy, M J; Crowley, L J; Roper, D et al. (2006) Identification and characterization of the novel FAD-binding lobe G75S mutation in cytochrome b(5) reductase: an aid to determine recessive congenital methemoglobinemia status in an infant. Blood Cells Mol Dis 36:81-90
Roma, Glenn W; Crowley, Louis J; Barber, Michael J (2006) Expression and characterization of a functional canine variant of cytochrome b5 reductase. Arch Biochem Biophys 452:69-82
Roma, Glenn W; Crowley, Louis J; Davis, C Ainsley et al. (2005) Mutagenesis of Glycine 179 modulates both catalytic efficiency and reduced pyridine nucleotide specificity in cytochrome b5 reductase. Biochemistry 44:13467-76
Percy, M J; Crowley, L J; Davis, C A et al. (2005) Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase. Br J Haematol 129:847-53
Marohnic, Christopher C; Crowley, Louis J; Davis, C Ainsley et al. (2005) Cytochrome b5 reductase: role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis. Biochemistry 44:2449-61
Davis, C Ainsley; Barber, Michael J (2004) Cytochrome b5 oxidoreductase: expression and characterization of the original familial ideopathic methemoglobinemia mutations E255- and G291D. Arch Biochem Biophys 425:123-32
Davis, C Ainsley; Crowley, Louis J; Barber, Michael J (2004) Cytochrome b5 reductase: the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*. Arch Biochem Biophys 431:233-44
Pollock, Veronica V; Conover, Richard C; Johnson, Michael K et al. (2003) Biotin sulfoxide reductase: Tryptophan 90 is required for efficient substrate utilization. Arch Biochem Biophys 409:315-26
Bewley, Maria C; Davis, C Ainsley; Marohnic, Christopher C et al. (2003) The structure of the S127P mutant of cytochrome b5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site. Biochemistry 42:13145-51

Showing the most recent 10 out of 63 publications