FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1973262186> ?p ?o ?g. }

• W1973262186 endingPage "940" @default.
• W1973262186 startingPage "925" @default.
• W1973262186 abstract "Nitrophorin 3 (NP3) is the only one of the four major NO-binding heme proteins found in the saliva of the blood-sucking insect Rhodnius prolixus (also called the Kissing Bug) for which it has not been possible to obtain crystals of diffraction quality for structure determination by X-ray crystallography. Thus we have used NMR spectroscopy, mainly of the hyperfine-shifted ferriheme substituent resonances, to learn about the similarities and differences in the heme pocket and the iron active site of NP3 as compared to NP2, which has previously been well-characterized by both X-ray crystallography and NMR spectroscopy. Only one residue in the heme pocket differs between the two, F27 of NP2 is Y27 for NP3; in both cases this residue is expected to interact strongly with the 2-vinyl side chain of the B heme rotational isomer or the 4-vinyl of the A heme rotational isomer. Both the high-spin (S = 5/2) aquo complex, NP3-H2O, and the low-spin (S = 1/2) N-methylimidazole (NMeIm) complex of NP3 have been studied. It is found that the chemical shifts of the protons of both forms are similar to those of the corresponding NP2 complexes, but with minor differences that indicate a slightly different angle for the proximal histidine (H57) ligand plane. The B heme rotational isomer is preferred by both NP3 and NP2 in both spin states, but to a greater extent when phenylalanine is present at position 27 (A:B = 1:8 for NP2, 1:6 for NP3-Y27F, 1:4 for NP3, and 1:3 for NP2-F27Y). Careful analysis of the 5Me and 8Me shifts of the A and B isomers of the two high-spin nitrophorins leads to the conclusion that the heme environment for the two isomers differs in some way that cannot be explained at the present time. The kinetics of deprotonation of the aquo ligand of the high-spin complexes of NP2 and NP3 are very different, with NP2 giving well-resolved high-spin aquo and “low-spin” hydroxo proton NMR spectra until close to the end of the titration, while NP3 exhibits broadened 1H NMR spectra indicative of an intermediate-rate of exchange on the NMR timescale between the two forms throughout the titration. The heme methyl shifts of NP2–OH are similar in magnitude and spread to those of NP2–CN, while those of metmyoglobin-hydroxo complexes are much larger in magnitude but not spread. It is concluded that the hydroxo complex of NP2 is likely S = 1/2 with a mixed(dxy)2(dxz, dyz)3/(dxy)1(dxz, dyz)4 electron configuration, while those of metMb–OH are likely S = 1/2,3/2 mixed spin systems." @default.
• W1973262186 created "2016-06-24" @default.
• W1973262186 creator A5007172461 @default.
• W1973262186 creator A5009032111 @default.
• W1973262186 creator A5011650766 @default.
• W1973262186 creator A5041572696 @default.
• W1973262186 creator A5054464320 @default.
• W1973262186 date "2008-03-01" @default.
• W1973262186 modified "2023-10-18" @default.
• W1973262186 title "Assignment of ferriheme resonances for high- and low-spin forms of nitrophorin 3 by 1H and 13C NMR spectroscopy and comparison to nitrophorin 2: Heme pocket structural similarities and differences" @default.
• W1973262186 cites W116505382 @default.
• W1973262186 cites W1509862190 @default.
• W1973262186 cites W1543239103 @default.
• W1973262186 cites W1545245178 @default.
• W1973262186 cites W1576996354 @default.
• W1973262186 cites W1628579658 @default.
• W1973262186 cites W1964263291 @default.
• W1973262186 cites W1966822141 @default.
• W1973262186 cites W1969318838 @default.
• W1973262186 cites W1969699979 @default.
• W1973262186 cites W1969737762 @default.
• W1973262186 cites W1973015058 @default.
• W1973262186 cites W1973483362 @default.
• W1973262186 cites W1974068717 @default.
• W1973262186 cites W1977414251 @default.
• W1973262186 cites W1989565215 @default.
• W1973262186 cites W1990748283 @default.
• W1973262186 cites W1991043991 @default.
• W1973262186 cites W2001298923 @default.
• W1973262186 cites W2003537955 @default.
• W1973262186 cites W2008083846 @default.
• W1973262186 cites W2010105986 @default.
• W1973262186 cites W2011725053 @default.
• W1973262186 cites W2012667043 @default.
• W1973262186 cites W2013041880 @default.
• W1973262186 cites W2016140160 @default.
• W1973262186 cites W2018737525 @default.
• W1973262186 cites W2020504230 @default.
• W1973262186 cites W2024390405 @default.
• W1973262186 cites W2027638545 @default.
• W1973262186 cites W2027766095 @default.
• W1973262186 cites W2028210963 @default.
• W1973262186 cites W2030422668 @default.
• W1973262186 cites W2034486610 @default.
• W1973262186 cites W2037943255 @default.
• W1973262186 cites W2038700761 @default.
• W1973262186 cites W2039247008 @default.
• W1973262186 cites W2041178006 @default.
• W1973262186 cites W2043596990 @default.
• W1973262186 cites W2044747737 @default.
• W1973262186 cites W2045426200 @default.
• W1973262186 cites W2048240651 @default.
• W1973262186 cites W2048711222 @default.
• W1973262186 cites W2054682788 @default.
• W1973262186 cites W2058622491 @default.
• W1973262186 cites W2063604622 @default.
• W1973262186 cites W2072454901 @default.
• W1973262186 cites W2072654567 @default.
• W1973262186 cites W2073141866 @default.
• W1973262186 cites W2075150947 @default.
• W1973262186 cites W2079193399 @default.
• W1973262186 cites W2081611819 @default.
• W1973262186 cites W2082979623 @default.
• W1973262186 cites W2083864143 @default.
• W1973262186 cites W2087734158 @default.
• W1973262186 cites W2110224127 @default.
• W1973262186 cites W2111371750 @default.
• W1973262186 cites W2112413125 @default.
• W1973262186 cites W2115070628 @default.
• W1973262186 cites W2122818112 @default.
• W1973262186 cites W2142550798 @default.
• W1973262186 cites W2145385387 @default.
• W1973262186 cites W2150046788 @default.
• W1973262186 cites W2158476620 @default.
• W1973262186 cites W2158798353 @default.
• W1973262186 cites W2952831323 @default.
• W1973262186 cites W3202761516 @default.
• W1973262186 doi "https://doi.org/10.1016/j.ica.2007.05.044" @default.
• W1973262186 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2390817" @default.
• W1973262186 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19262680" @default.
• W1973262186 hasPublicationYear "2008" @default.
• W1973262186 type Work @default.
• W1973262186 sameAs 1973262186 @default.
• W1973262186 citedByCount "18" @default.
• W1973262186 countsByYear W19732621862012 @default.
• W1973262186 countsByYear W19732621862013 @default.
• W1973262186 countsByYear W19732621862014 @default.
• W1973262186 crossrefType "journal-article" @default.
• W1973262186 hasAuthorship W1973262186A5007172461 @default.
• W1973262186 hasAuthorship W1973262186A5009032111 @default.
• W1973262186 hasAuthorship W1973262186A5011650766 @default.
• W1973262186 hasAuthorship W1973262186A5041572696 @default.
• W1973262186 hasAuthorship W1973262186A5054464320 @default.
• W1973262186 hasBestOaLocation W19732621862 @default.
• W1973262186 hasConcept C103319777 @default.
• W1973262186 hasConcept C116569031 @default.
• W1973262186 hasConcept C121332964 @default.
• W1973262186 hasConcept C170493617 @default.

• next