Blue transient complex formation in the electron–transfer reaction between iron(III) and a reduced nicotinamide–adenine dinucleotide analogue without an amide group

1990 ◽  
pp. 695-697 ◽  
Author(s):  
Shunichi Fukuzumi ◽  
Seiji Mochizuki ◽  
Toshio Tanaka
Keyword(s):  
Electron Transfer ◽  
Complex Formation ◽  
Nicotinamide Adenine Dinucleotide ◽  
Transfer Reaction ◽  
Electron Transfer Reaction ◽  
Amide Group ◽  
Nicotinamide Adenine ◽  
Transient Complex ◽  
Reduced Nicotinamide Adenine Dinucleotide

scholarly journals Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System

Biomolecules ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 826
Author(s):  
Noriyuki Nagahara
Keyword(s):  
Oxidative Stress ◽  
Electron Transfer ◽  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Transfer Reaction ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Electron Transfer Reaction ◽  
Reduced Form ◽  
Mercaptopyruvate Sulfurtransferase ◽  
Substrate Proteins

Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant Escherichia coli glutaredoxin1 (Cys14 is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.

An electron transfer reaction of a selenium coronand-copper(II) complex. Formation of the stable 1,5,9,13-tetraselenacyclohexadecane dication

1990 ◽  
Vol 112 (9) ◽  
pp. 3706-3707 ◽  
Author(s):  
Raymond J. Batchelor ◽  
Frederick W. B. Einstein ◽  
Ian D. Gay ◽  
Jian Hua Gu ◽  
B. Mario Pinto ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Complex Formation ◽  
Transfer Reaction ◽  
Electron Transfer Reaction

Charge-transfer complex formation and photo-induced electron-transfer reaction of dibenzo-7-silabicyclo[2.2.1]hepta-2,5-dienes

Tetrahedron ◽  
1997 ◽  
Vol 53 (4) ◽  
pp. 1265-1274 ◽  
Author(s):  
Masahiro Kako ◽  
Masahiro Mori ◽  
Kaname Hatakenaka ◽  
Seiji Kakuma ◽  
Yasuhiro Nakadaira ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Charge Transfer ◽  
Complex Formation ◽  
Transfer Reaction ◽  
Charge Transfer Complex ◽  
Electron Transfer Reaction ◽  
Photo Induced Electron Transfer
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