Exploring the Conformational Variability in the Heme b Propionic Acid Side Chains through the Effect of a Biological Probe: A Study of the Isolated Ions

2015 ◽  
Vol 119 (5) ◽  
pp. 1919-1929 ◽  
Author(s):  
Alberto De Petris ◽  
Barbara Chiavarino ◽  
Maria Elisa Crestoni ◽  
Cecilia Coletti ◽  
Nazzareno Re ◽  
...  
Keyword(s):  
Propionic Acid ◽  
Side Chains ◽  
Conformational Variability ◽  
Biological Probe

A mechanistic study of the reaction of iron (III) porphyries with imidazoles. Hydrogen bonding by the propionic acid side chains in hemin chloride

1985 ◽  
pp. 2269 ◽  
Author(s):  
Meng Qing-jin ◽  
Gerard A. Tondreau ◽  
John O. Edwards ◽  
Dwight A. Sweigart
Keyword(s):  
Hydrogen Bonding ◽  
Propionic Acid ◽  
Mechanistic Study ◽  
Side Chains ◽  
Hemin Chloride

scholarly journals The 3H-labelling of bilirubin

1976 ◽  
Vol 157 (2) ◽  
pp. 511-512 ◽  
Author(s):  
F E Hancock ◽  
D W Hutchinson ◽  
A J Knell
Keyword(s):  
Propionic Acid ◽  
Dimethyl Ester ◽  
Side Chains ◽  
Simple Method

A simple method has been developed for the preparation of 3H-labelled bilirubin IX-alpha from bilirubin dimethyl ester. The label is located in the propionic acid side chains, and there is no isomerization of the bilirubin during the preparation.

Synthesis of a hemin with structurally equivalent propionic acid side chains: 2,4-dimethyldeuterohemin IX dimethyl ester

1976 ◽  
Vol 5 (4) ◽  
pp. 325-327 ◽  
Author(s):  
Sally E. Parker ◽  
William S. Brinigar
Keyword(s):  
Propionic Acid ◽  
Dimethyl Ester ◽  
Side Chains

Synthesis and conformation of a bilirubin analog with propionic acid side chains extended to undecanoic acid

Tetrahedron ◽  
1992 ◽  
Vol 48 (29) ◽  
pp. 5969-5984 ◽  
Author(s):  
John Chiefari ◽  
Richard V. Person ◽  
David A. Lightner
Keyword(s):  
Propionic Acid ◽  
Side Chains ◽  
Undecanoic Acid

scholarly journals THE PORPHYRIN REQUIREMENTS OF HAEMOPHILUS INFLUENZAE AND SOME FUNCTIONS OF THE VINYL AND PROPIONIC ACID SIDE CHAINS OF HEME

1946 ◽  
Vol 30 (1) ◽  
pp. 1-13 ◽  
Author(s):  
S. Granick ◽  
H. Gilder
Keyword(s):  
Propionic Acid ◽  
Protoporphyrin Ix ◽  
Anomalous Behavior ◽  
Side Chains ◽  
Iron Porphyrins ◽  
Heme Enzymes ◽  
Low Concentrations ◽  
Rough Strain ◽  
Growth Promoting ◽  
Iron Protoporphyrin

1. Iron protoporphyrin IX was required for the growth of H. influenzae. It could be replaced by protoporphyrin IX. When grown on protoporphyrin evidence was obtained for the presence of Fe porphyrin in the organism. It was concluded that the organism could insert iron into the protoporphyrin ring. 2. In the smooth strains, other porphyrins containing no iron such as deutero-, hemato-, meso-, and coproporphyrins could not replace protoporphyrin for growth. Since protoporphyrin has two vinyl groups which other porphyrins lack, it was concluded that the two vinyl groups were essential for growth. 3. When porphyrins lacking vinyl groups were converted chemically into iron porphyrins and then supplied to the organisms it was found that these iron porphyrins supported growth. It was concluded that the "smooth" organisms were able to insert iron only into the porphyrin containing the vinyl groups; i.e., protoporphyrin. One function of the vinyl groups then was to permit iron to be inserted biologically into the porphyrin ring. 4. An anomalous behavior in the rough Turner strain was observed and discussed. This organism was able to insert iron into mesoporphyrin at low concentrations but was inhibited by this compound at higher concentrations. In all other reactions with the porphyrins this rough strain behaved in the same was as did the smooth strains. 5. All strains which were grown on iron porphyrins lacking vinyl groups could not reduce nitrate to nitrite. When grown on protoporphyrin or Fe protoporphyrin reduction of nitrate occurred. It was concluded that the nitrate-reducing mechanism required the presence of the vinyl groups either for its formation or function. 6. The porphyrins lacking iron and lacking vinyl groups inhibited the growth of H. influenzae on Fe protoporphyrin. The inhibition between a porphyrin and Fe protoporphyrin was a competitive one. It was suggested that the porphyrin inhibited the growth-promoting properties of Fe protoporphyrin by attaching on to a particular apoprotein, thus preventing the formation of a heme catalyst. Likewise, competition between two growth-promoting Fe porphyrins for apoenzymes could be shown to occur. 7. Protoporphyrin and Fe protoporphyrin supported growth. When their propionic acid side chains were esterified they no longer supported growth. It was suggested that the esterified carboxyl groups could not attach to the specific apoproteins to form the heme enzymes and so could not act to support growth. For the same reason the inhibitory action of porphyrins lacking vinyl groups could be prevented by esterifying their propionic acid groups.

ChemInform Abstract: Synthesis and Conformation of a Bilirubin Analogue with Propionic Acid Side Chains Extended to Undecanoic Acid.

ChemInform ◽  
2010 ◽  
Vol 23 (45) ◽  
pp. no-no
Author(s):  
J. CHIEFARI ◽  
R. V. PERSON ◽  
D. A. LIGHTNER
Keyword(s):  
Propionic Acid ◽  
Side Chains ◽  
Undecanoic Acid

The Effect of Halogen Substitution on the Side Chains of Discotic Liquid Crystals

1990 ◽  
Vol 182 (1) ◽  
pp. 201-207 ◽  
Author(s):  
C. P. Lillya ◽  
D. M. Collard
Keyword(s):  
Liquid Crystals ◽  
Side Chains ◽  
Discotic Liquid Crystals

Propionic acid as a precursor in the biosynthesis of animal fatty acids

1961 ◽  
Author(s):  
E.J. Masoro ◽  
Edith Porter
Keyword(s):  
Fatty Acids ◽  
Propionic Acid

Influence of Flexible Side-Chains on the Breathing Phase Transition of Pillared Layer MOFs: A Force Field Investigation

2020 ◽  
Author(s):  
Julian Keupp ◽  
Johannes P. Dürholt ◽  
Rochus Schmid
Keyword(s):  
First Principles ◽  
Good Accuracy ◽  
Field Investigation ◽  
Square Lattice ◽  
Side Chain ◽  
Second Step ◽  
Side Chains ◽  
Dynamics Simulations ◽  
Complex Phenomena ◽  
Closed Pore

The prototypical pillared layer MOFs, formed by a square lattice of paddle-<br>wheel units and connected by dinitrogen pillars, can undergo a breathing phase<br>transition by a “wine-rack” type motion of the square lattice. We studied this not<br>yet fully understood behavior using an accurate first principles parameterized force<br>field (MOF-FF) for larger nanocrystallites on the example of Zn 2 (bdc) 2 (dabco) [bdc:<br>benzenedicarboxylate, dabco: (1,4-diazabicyclo[2.2.2]octane)] and found clear indi-<br>cations for an interface between a closed and an open pore phase traveling through<br>the system during the phase transformation [Adv. Theory Simul. 2019, 2, 11]. In<br>conventional simulations in small supercells this mechanism is prevented by periodic<br>boundary conditions (PBC), enforcing a synchronous transformation of the entire<br>crystal. Here, we extend this investigation to pillared layer MOFs with flexible<br>side-chains, attached to the linker. Such functionalized (fu-)MOFs are experimen-<br>tally known to have different properties with the side-chains acting as fixed guest<br>molecules. First, in order to extend the parameterization for such flexible groups,<br>1a new parametrization strategy for MOF-FF had to be developed, using a multi-<br>structure force based fit method. The resulting parametrization for a library of<br>fu-MOFs is then validated with respect to a set of reference systems and shows very<br>good accuracy. In the second step, a series of fu-MOFs with increasing side-chain<br>length is studied with respect to the influence of the side-chains on the breathing<br>behavior. For small supercells in PBC a systematic trend of the closed pore volume<br>with the chain length is observed. However, for a nanocrystallite model a distinct<br>interface between a closed and an open pore phase is visible only for the short chain<br>length, whereas for longer chains the interface broadens and a nearly concerted trans-<br>formation is observed. Only by molecular dynamics simulations using accurate force<br>fields such complex phenomena can be studied on a molecular level.

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