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Kinetics and equilibria in ligand binding by nitrophorins 1-4: evidence for stabilization of a nitric oxide-ferriheme complex through a ligand-induced conformational trap.
TLDR
The results suggest that tighter NO binding in the nitrophorins is due to the trapping of the molecule in a nonpolar distal pocket rather than through formation of particularly strong Fe-NO or hydrogen bonds. Expand
Nitric Oxide Binding to the Ferri- and Ferroheme States of Nitrophorin 1, a Reversible NO-Binding Heme Protein from the Saliva of the Blood-Sucking Insect, Rhodnius prolixus
The recombinant NO-binding heme protein, nitrophorin 1 (NP1) from the saliva of the blood-sucking insect, Rhodnius prolixus, has been studied by spectroelectrochemistry, EPR, NMR, and FTIRExpand
The crystal structure of nitrophorin 4 at 1.5 A resolution: transport of nitric oxide by a lipocalin-based heme protein.
TLDR
The recombinant nitrophorin 4 structure is considerably higher resolution, confirms the unusual placement of ionizable groups in the protein interior, and clarifies the solvent arrangement in the distal pocket, and provides a striking example of structural homology where sequence homology is minimal. Expand
Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1.
TLDR
The side chain of residue 478 appears to be a major determinant of enzyme inactivation as well as of androgen hydroxylation in COS cell microsomes. Expand
Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus.
TLDR
These factors are consistent with nitrophorin function: NO storage in the apparent low pH of insect salivary glands and NO release into the tissue of the insect's host, where vasodilation is induced. Expand
Assignment of the ferriheme resonances of the low-spin complexes of nitrophorins 1 and 4 by (1)H and (13)C NMR spectroscopy: comparison to structural data obtained from X-ray crystallography.
TLDR
The three-dimensional structures of the three NP-CN complexes, including that of NP2-CN reported herein, confirm the high degree of ruffling of these complexes and can be much more accurately measured by NMR spectroscopy than by X-ray crystallography. Expand
Molecular basis for a functionally unique cytochrome P450IIB1 variant.
TLDR
Heterologous expression of P450 IIB1 and P450IIB1-WM confirmed the striking difference in androstenedione metabolite profiles, strongly implicating the involvement of Ala-478 in defining the distinctive catalytic properties of P 450IIB 1-WM. Expand
Isozyme selectivity of the inhibition of rat liver cytochromes P-450 by chloramphenicol in vivo.
TLDR
P-450PB-C, an isozyme which is present in significant amounts in untreated rats and which is induced approximately 2-fold by phenobarbital, was the most susceptible cytochrome P-450 to inhibition by chloramphenicol both in vivo and in vitro. Expand
Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: Stability, structure, and dynamics of axial ligand complexes
TLDR
NMR spectroscopic investigations show that the sterically demanding 2-methylimidazole ligand readily binds to all three distal pocket mutants to create low-spin Fe(III) complexes having axial ligands in nearly perpendicular planes; it also binds to the WT protein in the presence of higher concentrations of 2- methylimids, but yields a different ligand plane orientation than is present in any of the three distals pocket mutants. Expand
Dichloromethyl compounds as mechanism-based inactivators of rat liver cytochromes P-450 in vitro.
TLDR
The studies help delineate the structural requirements for the use of dichloromethyl compounds as probes of cytochrome P-450 function and as potential isozyme-selective inhibitors. Expand
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