Hydrogen bonding to the proximal imidazole in heme protein model compounds: effects upon oxygen binding and peroxidase activity

1988 ◽  
Vol 110 (1) ◽  
pp. 239-243 ◽  
Author(s):  
Teddy G. Traylor ◽  
Ronit. Popovitz-Biro
Keyword(s):  
Hydrogen Bonding ◽  
Peroxidase Activity ◽  
Heme Protein ◽  
Oxygen Binding ◽  
Model Compounds ◽  
Protein Model

An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization

2015 ◽  
Vol 13 (17) ◽  
pp. 4859-4868 ◽  
Author(s):  
Rosa Vitale ◽  
Liliana Lista ◽  
Corinne Cerrone ◽  
Giorgio Caserta ◽  
Marco Chino ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Structural Characterization ◽  
Peroxidase Activity ◽  
Heme Protein ◽  
Functional Screening ◽  
Heme Enzyme ◽  
Protein Model ◽  
Rational Refinement

The rational refinement of function into the heme-protein model Mimochrome VI (MC6) resulted in a new analogue, FeIII-E2L(TD)-MC6, with an improved peroxidase activity.

Seven-Membered Intramolecular Hydrogen Bonding of Phenols: Database Analysis and Phloroglucinol Model Compounds

2012 ◽  
Vol 2012 (24) ◽  
pp. 4483-4492 ◽  
Author(s):  
Ronald K. Castellano ◽  
Yan Li ◽  
Edwin A. Homan ◽  
Andrew J. Lampkins ◽  
Iris V. Marín ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Intramolecular Hydrogen Bonding ◽  
Model Compounds ◽  
Database Analysis ◽  
Intramolecular Hydrogen

scholarly journals Spectroscopic and kinetic properties of an oxygen-binding heme protein from Chromatium vinosum.

1987 ◽  
Vol 262 (3) ◽  
pp. 1144-1147
Author(s):  
D F Gaul ◽  
M R Ondrias ◽  
E W Findsen ◽  
G Palmer ◽  
J S Olson ◽  
...  
Keyword(s):  
Heme Protein ◽  
Chromatium Vinosum ◽  
Kinetic Properties ◽  
Oxygen Binding

Dual pathways of heme protein model compound reactions with carbon monoxide

1976 ◽  
Vol 98 (11) ◽  
pp. 3395-3396 ◽  
Author(s):  
John Cannon ◽  
Jon Geibel ◽  
Martha Whipple ◽  
T. G. Traylor
Keyword(s):  
Carbon Monoxide ◽  
Model Compound ◽  
Heme Protein ◽  
Protein Model

Bioenergy from Food Wastes: Thermal Decomposition of Carbohydrates, Lipids, and Proteins

2018 ◽  
Vol 61 (3) ◽  
pp. 797-805
Author(s):  
Zixu Yang ◽  
Jacob Collins ◽  
Ajay Kumar ◽  
Danielle Bellmer ◽  
Tim Bowser
Keyword(s):  
Activation Energy ◽  
Simple Structure ◽  
Reaction Scheme ◽  
Food Wastes ◽  
Model Compounds ◽  
Pyrolysis Products ◽  
Decomposition Scheme ◽  
Food Components ◽  
Protein Model ◽  
Single Reaction

Abstract. Food wastes differ in composition based on their sources and hence are difficult to use in gasification and pyrolysis technologies. The objectives of this study were to investigate the thermal devolatilization kinetics and pyrolysis products of three representative food components: lipids, carbohydrates, and protein. Devolatilization of carbohydrates and proteins occurred up to 600°C with a total weight loss of 90%. In particular, dextrose, sucrose, histidine, and phenylalanine exhibited a combined two-reaction decomposition scheme, whereas starch and valine exhibited a single-reaction scheme. Sucrose had a higher activation energy than dextrose as more energy was needed to cleave glyosidic linkages. Valine had the lowest activation energy (70.2 kJ mol-1) of all the protein model compounds due to its simple structure. However, the lipids primarily vaporized below 400°C and did not decompose. Pyrolysis products of carbohydrates were largely composed of furan and sugar-based compounds, whereas those of proteins varied depending on the type of protein. Because lipids mainly vaporized, only slight conversion (<1%) into different lipid types and hydrocarbons was observed. Keywords: Carbohydrate, Devolatilization, Food waste, Lipid, Protein, Py-GC/MS, Pyrolysis, Reaction kinetics, TGA.

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