ArticleBiochemistry2007
Effect of the N-terminus on heme cavity structure, ligand equilibrium, rate constants, and reduction potentials of nitrophorin 2 from Rhodnius prolixus.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferrihemeChemical science · 2016Article
- Dimerization of nitrophorin 4 at low pH and comparison to the K1A mutant of nitrophorin 1.Biochemistry · 2015Article
- NMR studies of the dynamics of high-spin nitrophorins: comparative studies of NP4 and NP2 at close to physiological pH.Biochemistry · 2015Article
- Kinetic results for mutations of conserved residues H304 and R309 of human sulfite oxidase point to mechanistic complexities.Metallomics : integrated biometal science · 2014Article
- NMR investigations of nitrophorin 2 belt side chain effects on heme orientation and seating of native N-terminus NP2 and NP2(D1A).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- NMR studies of the dynamics of nitrophorin 2 bound to nitric oxide.Biochemistry · 2013Article
- Probing the role of a conserved salt bridge in the intramolecular electron transfer kinetics of human sulfite oxidase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Electron spin density on the axial His ligand of high-spin and low-spin nitrophorin 2 probed by heteronuclear NMR spectroscopy.Inorganic chemistry · 2013Article
- Native N-terminus nitrophorin 2 from the kissing bug: similarities to and differences from NP2(D1A).Chemistry & biodiversity · 2012Article
- Assignment of the 1H NMR resonances of protein residues in close proximity to the heme of the nitrophorins: similarities and differences among the four proteins from the saliva of the adult blood-sucking insect Rhodnius prolixus.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Tyrosine triad at the interface between the Rieske iron-sulfur protein, cytochrome c1 and cytochrome c2 in the bc1 complex of Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Article
- Nuclear inelastic scattering and Mössbauer spectroscopy as local probes for ligand binding modes and electronic properties in proteins: vibrational behavior of a ferriheme center inside a β-barrel protein.Journal of the American Chemical Society · 2012Article
- Intramolecular electron transfer in sulfite-oxidizing enzymes: probing the role of aromatic amino acids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- NMR studies of nitrophorin distal pocket side chain effects on the heme orientation and seating of NP2 as compared to NP1.Journal of inorganic biochemistry · 2011Article
- Elucidating the catalytic mechanism of sulfite oxidizing enzymes using structural, spectroscopic, and kinetic analyses.Biochemistry · 2010Review
- Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase.Biochemistry · 2010Article
- 1H and 13C NMR spectroscopic studies of the ferriheme resonances of three low-spin complexes of wild-type nitrophorin 2 and nitrophorin 2(V24E) as a function of pH.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009Article
- Effect of mutation of carboxyl side-chain amino acids near the heme on the midpoint potentials and ligand binding constants of nitrophorin 2 and its NO, histamine, and imidazole complexes.Journal of the American Chemical Society · 2009Article
- Assignment of the ferriheme resonances of high- and low-spin forms of the symmetrical hemin-reconstituted nitrophorins 1-4 by 1H and 13C NMR spectroscopy: the dynamics of heme ruffling deformations.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2008Article
- Assignment of Ferriheme Resonances for High- and Low-Spin Forms of Nitrophorin 3 by H and C NMR Spectroscopy and Comparison to Nitrophorin 2: Heme Pocket Structural Similarities and Differences.Inorganica chimica acta · 2008Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The D1A mutant of recombinant NP2 has been prepared and shown to have the expression-initiation methionine-0 cleaved during expression in E. coli, as is the case for recombinant NP4, where Ala is the first amino acid for the recombinant protein as well as for the mature native protein. The heme substituent 1H NMR chemical shifts of NP2-D1A and those of its imidazole, N-methylimidazole, and cyanide complexes are rather different from those of NP2-M0D1. This difference is likely due to the much smaller size of the N-terminal amino acid (A) of NP2-D1A, which allows the formation of the closed loop form of this protein, as it does for NP4 (Weichsel, A., Andersen, J. F., Roberts, S. A., and Montfort, W. R. (2000) Nature Struct. Biol. 7, 551-554). The ratio of the two hemin rotational isomers A and B is different for the two proteins, and the rate at which the A:B ratio reaches equilibrium is strikingly different (NP2-M0D1 t1/2 for heme rotation approximately 2 h, NP2-D1A t1/2 approximately 43 h). This difference is consistent with the high stability of the closed loop form of the NP2-D1A protein and infrequent opening of the loops that could allow heme to at least partially exit the binding pocket in order to rotate about its alpha,gamma-meso axis. Consistent with this, the rates of histamine binding and release to/from NP2-D1A are significantly slower than those for NP2-M0D1 at pH 7.5. This work suggests that care must be taken in interpreting data obtained from proteins that carry the expression-initiation M0.
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