Search Within
Applied Filters:
Showing 1-24 of 24 results for "


" within Papers
Sort by Relevance
Y Imai et al.
Biochimica et biophysica acta, 1207(1), 49-57 (1994-07-20)
Thr-303 to Lys-mutated P-450 2E1, as well as Thr-301 to Lys-mutated P-450 2C2, had absorption spectra characteristic of a nitrogenous ligand-bound form of P-450, such as the pyridine complex of P-450 2E1; (i) in the ferric state, the red-shifted Soret
Effect of isocyanide on the ultrastructure of mouse pineal.
N Chang et al.
Anatomia, histologia, embryologia, 13(2), 181-188 (1984-06-01)
Robert D Smith et al.
Biochemistry, 49(24), 4977-4986 (2010-05-21)
Crystal structures of methyl, ethyl, propyl, and butyl isocyanide bound to sperm whale myoglobin (Mb) reveal two major conformations. In the in conformer, His(E7) is in a "closed" position, forcing the ligand alkyl chain to point inward. In the out
G A Bálint et al.
Acta medica Hungarica, 41(4), 247-252 (1984-01-01)
The microsomal fraction of the liver was studied for protein and cytochrome P450 contents as well as for aminopyrine-N-demethylase and aniline-hydroxylase activity and for its BIC spectrum under the effect of PG-I2 treatment. A significant increase was found in the
Alessandra Pesce et al.
Methods in enzymology, 436, 303-315 (2008-02-02)
Protein matrix cavities and extended tunnels can effectively channel substrates and products to and from active sites in enzymes. Substrate and product channeling can enhance catalytic efficiency by reducing the intramolecular diffusion times to and from reaction centers. Moreover, protected
C Mouro et al.
FEBS letters, 455(3), 302-306 (1999-08-07)
A 1H nuclear magnetic resonance study of the complex of cytochrome P450cam-putidaredoxin has been performed. Isocyanide is bound to cytochrome P450cam in order to increase the stability of the protein both in the reduced and the oxidized state. Diprotein complex
T Tomita et al.
The Journal of biological chemistry, 276(39), 36261-36267 (2001-07-19)
Alkylisocyanide adducts of microsomal P450 exist in two interconvertible forms, each giving the Soret maximum around 430 or 455 nm. This is demonstrated with a rabbit liver P450 2B4. Resonance Raman spectra of the 430- and 455-nm forms were examined
J Doussière et al.
Biochemistry, 35(41), 13400-13410 (1996-10-15)
The NADPH oxidase complex of activated neutrophils consists of a membrane-bound flavocytochrome b and cytosolic activation factors. Despite its ability to react with O2, the heme b component of the flavocytochrome is insensitive to cyanide and CO2, and slowly reactive
Holger Dobbek et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(25), 15971-15976 (2002-12-12)
The CO dehydrogenase of the eubacterium Oligotropha carboxidovorans is a 277-kDa Mo- and Cu-containing iron-sulfur flavoprotein. Here, the enzyme's active site in the oxidized or reduced state, after inactivation with potassium cyanide or with n-butylisocyanide bound to the active site
Emily R Derbyshire et al.
The Journal of biological chemistry, 282(49), 35741-35748 (2007-10-06)
Nitric oxide (NO) is a physiologically relevant activator of the hemoprotein soluble guanylate cyclase (sGC). In the presence of NO, sGC is activated several hundredfold above the basal level by a mechanism that remains to be elucidated. The heme ligand
Sotaro Fujii et al.
Protein science : a publication of the Protein Society, 26(4), 737-748 (2017-01-18)
Thermophilic Hydrogenophilus thermoluteolus cytochrome c' (PHCP) exhibits higher thermal stability than a mesophilic counterpart, Allochromatium vinosum cytochrome c' (AVCP), which has a homo-dimeric structure and ligand-binding ability. To understand the thermal stability mechanism and ligand-binding ability of the thermally stable
Jae-Hun Jeoung et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 17(2), 167-173 (2011-09-10)
Carbon monoxide dehydrogenases (CODHs) catalyze the reversible oxidation of carbon monoxide by reaction with water to yield carbon dioxide, two protons, and two electrons. Two principal types of CODHs can be distinguished. Ni,Fe-containing CODHs contain a [NiFe(4)S(4)OH(x)] cluster within their
M J Patel et al.
The Biochemical journal, 262(3), 959-963 (1989-09-15)
Equilibrium constants for the binding of ethyl (EIC), n-butyl (BIC), p-toluenesulphonylmethyl (TMIC) and 2,6-dimethylphenyl isocyanides (DIMPI) to an imidazole-haem complex in toluene and aqueous detergent micelle solutions were determined. In contrast to an earlier study, which indicated that the large
J H Sommer et al.
Biochemistry, 24(25), 7380-7388 (1985-12-03)
Transient optical absorption spectra of myoglobin were measured following photolysis of the n-butyl isocyanide complex with 10-ns laser pulses at room temperature. The data were analyzed by using singular value decomposition to give the kinetics of ligand rebinding and spectral
Y Imai et al.
Biochimica et biophysica acta, 1337(1), 66-74 (1997-01-04)
Heme-external ligand interactions of P-450nor were examined spectrophotometrically and compared with those of other P-450s. Most nitrogenous ligands induced type II spectral changes on binding to ferric P-450nor, as did other P-450s. In contrast with other P-450s, 2-methylpyridine and 1-butanol
Akira Ikezaki et al.
Chemical communications (Cambridge, England), (19)(19), 2257-2259 (2008-05-09)
Addition of tert-butylisocyanide (tBuNC) to a CD2Cl2 solution of the bis(perchlorato)(meso-tetramesitylporphyrinato) iron(III) cation radical leads to the formation of the corresponding bis(adduct), [Fe(TMP)(tBuNC)2]2+, whose electronic structure is in sharp contrast to that of the corresponding imidazole(HIm) complex, [Fe(TMP)(HIm)2]2+; the former
B Giardina et al.
European journal of biochemistry, 135(1), 171-174 (1983-09-01)
Binding of alkylisocyanides of different bulkiness to the two major components of trout hemolysate is presented. In the case of trout hemoglobin I isocyanide binding is pH-independent, similar to O2 and CO, and the bulkiness of the ligand is related
T H Tahirov et al.
Nature structural biology, 3(5), 459-464 (1996-05-01)
We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c'. This is the first example of a ligand-bound structure of a class IIa cytochrome c. Compared with the structure of native cytochrome c', there are significant conformational changes of
Toshitada Yoshihara et al.
The journal of physical chemistry. A, 109(8), 1497-1509 (2006-07-13)
For the electron acceptor/donor molecule N-phenylpyrrole (PP), the fast intramolecular charge transfer (ICT) reaction accompanied by dual fluorescence from a locally excited (LE) and an ICT state is investigated in alkyl cyanide solvents as a function of temperature. After a
D S Lee et al.
Biochemistry, 40(9), 2669-2677 (2001-03-22)
Alkyl-isocyanides are able to bind to both ferric and ferrous iron of the heme in cytochrome P450, and the resulting complexes exhibit characteristic optical absorption spectra. While the ferric complex gives a single Soret band at 430 nm, the ferrous
C Mouro et al.
European journal of biochemistry, 267(1), 216-221 (1999-12-22)
An 1H-NMR study of ferric cytochrome P450cam in different paramagnetic states was performed. Assignment of three heme methyl resonances of the isocyanide adduct of cytochrome P450 in the ferric low-spin state was recently performed using electron exchange in the presence
D Barrick et al.
Biochemistry, 40(13), 3780-3795 (2001-04-13)
The linkage between the proximal histidines and the proximal polypeptide in normal adult human hemoglobin (Hb A) has been proposed to play a major role in transmitting allosteric effects between oxygen binding sites [Perutz, M. F. (1970) Nature 228, 726-734].
John P Evans et al.
Biochemistry, 48(37), 8920-8928 (2009-08-22)
Heme oxygenases (HO) catalyze the oxidative cleavage of heme to generate biliverdin, CO, and free iron. In humans, heme oxygenase-1 (hHO-1) is overexpressed in tumor tissues, where it helps to protect cancer cells from anticancer agents, while HOs in fungal
Kurtis M Carsch et al.
Science (New York, N.Y.), 365(6458), 1138-1143 (2019-09-14)
Terminal copper-nitrenoid complexes have inspired interest in their fundamental bonding structures as well as their putative intermediacy in catalytic nitrene-transfer reactions. Here, we report that aryl azides react with a copper(I) dinitrogen complex bearing a sterically encumbered dipyrrin ligand to
Page 1 of 1
Page 1 of 1