The ability of the NiSOD binding loop to chelate zinc(ii): the role of the terminal amino group in the enzymatic functions

2019 ◽  
Vol 48 (18) ◽  
pp. 6217-6227 ◽  
Author(s):  
Gizella Csire ◽  
András Kolozsi ◽  
Tamás Gajda ◽  
Giuseppe Pappalardo ◽  
Katalin Várnagy ◽  
...  
Keyword(s):  
Crucial Role ◽  
Spectroscopic Characterization ◽  
Amino Group ◽  
Amino Groups ◽  
Enzymatic Function ◽  
Terminal Amino ◽  
Binding Loop

Equilibrium and spectroscopic characterization of zinc(ii) complexes with NiSOD related peptides highlights the crucial role of terminal amino groups in the enzymatic function.

Spectroscopic characterization of free-base hydroxy(arylethynyl)porphyrins in acidic and basic media

2017 ◽  
Vol 21 (10) ◽  
pp. 680-691
Author(s):  
Kaarin K. Evens ◽  
Kathryn E. Splan
Keyword(s):  
Spectroscopic Characterization ◽  
Spectral Features ◽  
Free Base ◽  
Enhanced Absorption ◽  
Spectral Shifts ◽  
Porphyrin Macrocycle ◽  
Show Evidence ◽  
Acidic Conditions

The addition of arylethynyl groups to the porphyrin macrocycle represents an effective strategy with which to enhance the light-harvesting properties of porphyrins. We now extend this modification to arylethynyl porphyrins with two or four [Formula: see text]-hydroxyphenyl substituents. Arylethynyl porphyrins bearing four, but not two, [Formula: see text]-hydroxyphenyl substituents show evidence of aggregation under acidic conditions. Under basic conditions, deprotonation of the peripheral hydroxyphenyl substituents results in substantially red-shifted spectral features and enhanced absorption in the Q-band region. When the hydroxyphenyl groups are appended to the porphyrin macrocylce via the ethynyl spacers, the spectral shifts observed upon deprotonation are significantly enhanced relative to those observed for hydroxyphenylporphyrins, highlighting the role of expanded conjugation in altering porphyrin photophysics.

Dynamic Characterization of the Water Binding Loop in the P-Type Cardiotoxin:  Implication for the Role of the Bound Water Molecule†

Biochemistry ◽  
2001 ◽  
Vol 40 (43) ◽  
pp. 12782-12794 ◽  
Author(s):  
Shih-Che Sue ◽  
Harold C. Jarrell ◽  
Jean-Robert Brisson ◽  
Wen-guey Wu
Keyword(s):  
Water Molecule ◽  
Bound Water ◽  
Dynamic Characterization ◽  
Water Binding ◽  
P Type ◽  
Binding Loop

Application of Hyperbranched Polymer with Terminal Amino in Dyeing Process of Microfiber Synthetic Leather

2011 ◽  
Vol 393-395 ◽  
pp. 1114-1118
Author(s):  
Long Fang Ren ◽  
Guo Hui Zhao ◽  
Tao Tao Qiang ◽  
Jing Xian Wang ◽  
Xue Chuan Wang
Keyword(s):  
Uptake Rate ◽  
Hyperbranched Polymer ◽  
Succinic Anhydride ◽  
Amino Group ◽  
Dye Uptake ◽  
Amino Groups ◽  
Synthetic Leather ◽  
Dyeing Process ◽  
Terminal Amino ◽  
Polymerization Method

Hyperbranched polymer with different contents of terminal amino group synthesized with succinic anhydride and DETA through the molten polymerization method was used in the dying process of microfiber synthetic leather substrate as color fixing agent. The effect on dye-uptake, surface chromas of microfiber synthetic leather substrate, wet and dry rub fastness was discussed. The result indicated that when the dosage of hyperbranched polymer with 5.85% terminal amino groups was 0.8%, the dye uptake rate was 92.92% and surface chroma was the best, the wet and dry rub fastness of microfiber synthetic leather substrate were almost unchanged.

scholarly journals Structural and Spectroscopic Characterization of TPGS Micelles: Disruptive Role of Cyclodextrins and Kinetic Pathways

Langmuir ◽  
2017 ◽  
Vol 33 (19) ◽  
pp. 4737-4747 ◽  
Author(s):  
Joan Puig-Rigall ◽  
Isabelle Grillo ◽  
Cécile A. Dreiss ◽  
Gustavo González-Gaitano
Keyword(s):  
Spectroscopic Characterization

scholarly journals o-Quinones formed in plant extracts. Their reactions with amino acids and peptides

1969 ◽  
Vol 112 (5) ◽  
pp. 609-616 ◽  
Author(s):  
W. S. Pierpoint
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plant Extracts ◽  
Thiol Group ◽  
Amino Group ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Secondary Reactions ◽  
Terminal Amino ◽  
Group 5

1. The reactions of amino acids and peptides with the o-quinones produced by the enzymic oxidation of chlorogenic acid and caffeic acid have been studied manometrically and spectrophotometrically. 2. Amino acids, except lysine and cysteine, react primarily through their α-amino groups to give red or brown products. These reactions, which compete with the polymerization of the quinones, are followed by secondary reactions that may absorb oxygen and give products with other colours. 3. The ∈-amino group of lysine reacts with the o-quinones in a similar way. The thiol group of cysteine reacts with the quinones, without absorbing oxygen, giving colourless products. 4. Peptides containing cysteine react with the o-quinones through their thiol group. 5. Other peptides, such as glycyl-leucine and leucylglycine, react primarily through their α-amino group and the overall reaction resembles that of the N-terminal amino acid except that it is quicker. 6. With some peptides, the secondary reactions differ from those that occur between the o-quinones and the N-terminal amino acids. The colours produced from carnosine resemble those produced from histidine rather than those from β-alanine, and the reactions of prolylalanine with o-quinones are more complex than those of proline.

scholarly journals Spectroscopic Characterization of YedY: The Role of Sulfur Coordination in a Mo(V) Sulfite Oxidase Family Enzyme Form

2009 ◽  
Vol 131 (43) ◽  
pp. 15612-15614 ◽  
Author(s):  
Jing Yang ◽  
Richard Rothery ◽  
Joseph Sempombe ◽  
Joel H. Weiner ◽  
Martin L. Kirk
Keyword(s):  
Spectroscopic Characterization ◽  
Sulfite Oxidase ◽  
Enzyme Form
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